CPXB_PRIM2
ID CPXB_PRIM2 Reviewed; 1049 AA.
AC P14779; A0A0B6AQ66; Q9AE23;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000305};
DE AltName: Full=Cytochrome P450(BM-3) {ECO:0000303|PubMed:15299332};
DE AltName: Full=Cytochrome P450BM-3 {ECO:0000303|PubMed:8342039, ECO:0000312|EMBL:AAK19020.1};
DE AltName: Full=Fatty acid monooxygenase {ECO:0000303|PubMed:3106359};
DE AltName: Full=Flavocytochrome P450 BM3 {ECO:0000303|PubMed:11695889, ECO:0000303|PubMed:14653735};
DE Includes:
DE RecName: Full=Cytochrome P450 102A1;
DE EC=1.14.14.1 {ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};
DE Includes:
DE RecName: Full=NADPH--cytochrome P450 reductase;
DE EC=1.6.2.4 {ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};
GN Name=cyp102A1 {ECO:0000312|EMBL:AJI21949.1}; Synonyms=cyp102;
GN ORFNames=BG04_163 {ECO:0000312|EMBL:AJI21949.1};
OS Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 /
OS NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)
OS (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1348623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376
RC / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19
RC {ECO:0000303|PubMed:2544578};
RX PubMed=2544578; DOI=10.1016/s0021-9258(18)60416-8;
RA Ruettinger R.T., Wen L.-P., Fulco A.J.;
RT "Coding nucleotide, 5' regulatory, and deduced amino acid sequences of P-
RT 450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from
RT Bacillus megaterium.";
RL J. Biol. Chem. 264:10987-10995(1989).
RN [2] {ECO:0000312|EMBL:AJI21949.1, ECO:0000312|Proteomes:UP000031829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376
RC / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19
RC {ECO:0000312|EMBL:AJI21949.1};
RX PubMed=25931591; DOI=10.1128/genomea.00151-15;
RA Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G.,
RA Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Gibbons H.S.,
RA Coyne S.R., Lo C.C., Meincke L., Munk A.C., Koroleva G.I., Rosenzweig C.N.,
RA Palacios G.F., Redden C.L., Minogue T.D., Chain P.S.;
RT "Complete genome sequences for 35 biothreat assay-relevant bacillus
RT species.";
RL Genome Announc. 3:0-0(2015).
RN [3] {ECO:0000312|EMBL:AAK19020.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29, AND INDUCTION.
RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376
RC / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19
RC {ECO:0000303|PubMed:1544926};
RX PubMed=1544926; DOI=10.1016/s0021-9258(18)42797-4;
RA Shaw G.C., Fulco A.J.;
RT "Barbiturate-mediated regulation of expression of the cytochrome P450BM-3
RT gene of Bacillus megaterium by Bm3R1 protein.";
RL J. Biol. Chem. 267:5515-5526(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376
RC / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19
RC {ECO:0000303|PubMed:3106359};
RX PubMed=3106359; DOI=10.1016/s0021-9258(18)48295-6;
RA Wen L.P., Fulco A.J.;
RT "Cloning of the gene encoding a catalytically self-sufficient cytochrome P-
RT 450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium
RT and its functional expression and regulation in heterologous (Escherichia
RT coli) and homologous (Bacillus megaterium) hosts.";
RL J. Biol. Chem. 262:6676-6682(1987).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=1727637; DOI=10.1016/0003-9861(92)90045-x;
RA Boddupalli S.S., Pramanik B.C., Slaughter C.A., Estabrook R.W.,
RA Peterson J.A.;
RT "Fatty acid monooxygenation by P450BM-3: product identification and
RT proposed mechanisms for the sequential hydroxylation reactions.";
RL Arch. Biochem. Biophys. 292:20-28(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-75; PHE-88 AND
RP LEU-189.
RX PubMed=16566047; DOI=10.1002/cbic.200500444;
RA Budde M., Morr M., Schmid R.D., Urlacher V.B.;
RT "Selective hydroxylation of highly branched fatty acids and their
RT derivatives by CYP102A1 from Bacillus megaterium.";
RL ChemBioChem 7:789-794(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18020460; DOI=10.1021/bi701945j;
RA Chowdhary P.K., Keshavan N., Nguyen H.Q., Peterson J.A., Gonzalez J.E.,
RA Haines D.C.;
RT "Bacillus megaterium CYP102A1 oxidation of acyl homoserine lactones and
RT acyl homoserines.";
RL Biochemistry 46:14429-14437(2007).
RN [8] {ECO:0007744|PDB:2HPD}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-472 IN COMPLEX WITH HEME.
RX PubMed=8342039; DOI=10.1126/science.8342039;
RA Ravichandran K.G., Boddupalli S.S., Hasemann C.A., Peterson J.A.,
RA Deisenhofer J.;
RT "Crystal structure of hemoprotein domain of P450BM-3, a prototype for
RT microsomal P450's.";
RL Science 261:731-736(1993).
RN [9] {ECO:0007744|PDB:2BMH}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 IN COMPLEX WITH HEME.
RX PubMed=15299332; DOI=10.1107/s0907444994009194;
RA Li H., Poulos T.L.;
RT "Modeling protein-substrate interactions in the heme domain of cytochrome
RT P450(BM-3).";
RL Acta Crystallogr. D 51:21-32(1995).
RN [10] {ECO:0007744|PDB:1FAH}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-472 OF MUTANT ALA-269 IN COMPLEX
RP WITH HEME, CATALYTIC ACTIVITY, COFACTOR, SITE, AND MUTAGENESIS OF THR-269.
RX PubMed=7578081; DOI=10.1021/bi00045a014;
RA Yeom H., Sligar S.G., Li H., Poulos T.L., Fulco A.J.;
RT "The role of Thr268 in oxygen activation of cytochrome P450BM-3.";
RL Biochemistry 34:14733-14740(1995).
RN [11] {ECO:0007744|PDB:1FAG}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-472 IN COMPLEX WITH HEME AND
RP PALMITOLEIC ACID.
RX PubMed=9033595; DOI=10.1038/nsb0297-140;
RA Li H.Y., Poulos T.L.;
RT "The structure of the cytochrome p450BM-3 haem domain complexed with the
RT fatty acid substrate, palmitoleic acid.";
RL Nat. Struct. Biol. 4:140-146(1997).
RN [12] {ECO:0007744|PDB:1BU7, ECO:0007744|PDB:1BVY}
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-650 IN COMPLEX WITH FMN AND
RP HEME.
RX PubMed=10051560; DOI=10.1073/pnas.96.5.1863;
RA Sevrioukova I.F., Li H., Zhang H., Peterson J.A., Poulos T.L.;
RT "Structure of a cytochrome P450-redox partner electron-transfer complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1863-1868(1999).
RN [13] {ECO:0007744|PDB:1JME}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 OF MUTANT HIS-394 IN COMPLEX
RP WITH HEME, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-394.
RX PubMed=11695889; DOI=10.1021/bi010717e;
RA Ost T.W., Munro A.W., Mowat C.G., Taylor P.R., Pesseguiero A., Fulco A.J.,
RA Cho A.K., Cheesman M.A., Walkinshaw M.D., Chapman S.K.;
RT "Structural and spectroscopic analysis of the F393H mutant of
RT flavocytochrome P450 BM3.";
RL Biochemistry 40:13430-13438(2001).
RN [14] {ECO:0007744|PDB:1JPZ}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471 IN COMPLEX WITH HEME AND
RP N-PALMITOYLGLYCINE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11695892; DOI=10.1021/bi011197q;
RA Haines D.C., Tomchick D.R., Machius M., Peterson J.A.;
RT "Pivotal role of water in the mechanism of P450BM-3.";
RL Biochemistry 40:13456-13465(2001).
RN [15] {ECO:0007744|PDB:1P0V, ECO:0007744|PDB:1P0W, ECO:0007744|PDB:1P0X}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-456 OF MUTANTS ALA/TRP/TYR-394
RP IN COMPLEXES WITH HEME, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP PHE-394.
RX PubMed=14653735; DOI=10.1021/ja035731o;
RA Ost T.W., Clark J., Mowat C.G., Miles C.S., Walkinshaw M.D., Reid G.A.,
RA Chapman S.K., Daff S.;
RT "Oxygen activation and electron transfer in flavocytochrome P450 BM3.";
RL J. Am. Chem. Soc. 125:15010-15020(2003).
RN [16] {ECO:0007744|PDB:1SMI, ECO:0007744|PDB:1SMJ}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-472 OF MUTANT GLU-265 IN
RP COMPLEXES WITH HEME AND PALMITOLEIC ACID.
RX PubMed=15020590; DOI=10.1074/jbc.m401717200;
RA Joyce M.G., Girvan H.M., Munro A.W., Leys D.;
RT "A single mutation in cytochrome P450 BM3 induces the conformational
RT rearrangement seen upon substrate binding in the wild-type enzyme.";
RL J. Biol. Chem. 279:23287-23293(2004).
RN [17] {ECO:0007744|PDB:1YQO, ECO:0007744|PDB:1YQP}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-456 OF MUTANTS ALA/ASN-269 IN
RP COMPLEXES WITH HEME, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, ENZYME KINETICS, ABSORPTION SPECTROSCOPY, REDOX POTENTIOMETRY
RP OF HEME, AND MUTAGENESIS OF THR-269 AND PHE-394.
RX PubMed=16403573; DOI=10.1016/j.jinorgbio.2005.11.020;
RA Clark J.P., Miles C.S., Mowat C.G., Walkinshaw M.D., Reid G.A., Daff S.N.,
RA Chapman S.K.;
RT "The role of Thr268 and Phe393 in cytochrome P450 BM3.";
RL J. Inorg. Biochem. 100:1075-1090(2006).
RN [18] {ECO:0007744|PDB:1ZO9}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-471 IN COMPLEX WITH HEME AND
RP N-PALMITOYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ARG-48.
RX PubMed=18004886; DOI=10.1021/bi701667m;
RA Hegde A., Haines D.C., Bondlela M., Chen B., Schaffer N., Tomchick D.R.,
RA Machius M., Nguyen H., Chowdhary P.K., Stewart L., Lopez C., Peterson J.A.;
RT "Interactions of substrates at the surface of P450s can greatly enhance
RT substrate potency.";
RL Biochemistry 46:14010-14017(2007).
RN [19] {ECO:0007744|PDB:2J1M, ECO:0007744|PDB:2J4S}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-456 IN COMPLEXES WITH HEME.
RX PubMed=17429965; DOI=10.1021/ja067036x;
RA Kuper J., Wong T.S., Roccatano D., Wilmanns M., Schwaneberg U.;
RT "Understanding a mechanism of organic cosolvent inactivation in heme
RT monooxygenase P450 BM-3.";
RL J. Am. Chem. Soc. 129:5786-5787(2007).
RN [20] {ECO:0007744|PDB:2IJ2, ECO:0007744|PDB:2IJ3, ECO:0007744|PDB:2IJ4}
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 2-471 OF WILD-TYPE AND MUTANTS
RP HIS/LYS-265 IN COMPLEXES WITH HEME, FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ALA-265.
RX PubMed=17077084; DOI=10.1074/jbc.m607949200;
RA Girvan H.M., Seward H.E., Toogood H.S., Cheesman M.R., Leys D., Munro A.W.;
RT "Structural and spectroscopic characterization of P450 BM3 mutants with
RT unprecedented P450 heme iron ligand sets. New heme ligation states
RT influence conformational equilibria in P450 BM3.";
RL J. Biol. Chem. 282:564-572(2007).
RN [21] {ECO:0007744|PDB:2UWH}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-459 OF MUTANT PHE-83 IN COMPLEX
RP WITH HEME AND PALMITIC ACID, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS, AND MUTAGENESIS OF ALA-83.
RX PubMed=17868686; DOI=10.1016/j.jmb.2007.08.015;
RA Huang W.C., Westlake A.C., Marechal J.D., Joyce M.G., Moody P.C.,
RA Roberts G.C.;
RT "Filling a hole in cytochrome P450 BM3 improves substrate binding and
RT catalytic efficiency.";
RL J. Mol. Biol. 373:633-651(2007).
RN [22] {ECO:0007744|PDB:3BEN}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-470 IN COMPLEX WITH HEME AND
RP SUBSTRATE INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=18298086; DOI=10.1021/bi7023964;
RA Haines D.C., Chen B., Tomchick D.R., Bondlela M., Hegde A., Machius M.,
RA Peterson J.A.;
RT "Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of
RT substrate access channel.";
RL Biochemistry 47:3662-3670(2008).
RN [23] {ECO:0007744|PDB:3CBD}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-456 OF
RP MUTANT ALA-79/TYR-139/ILE-176/ILE-179/VAL-185/GLN-237/GLY-253/SER-256/VAL-
RP 291/THR-296/VAL-354 IN COMPLEX WITH HEME AND N-PALMITOYLGLYCINE, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=18619466; DOI=10.1016/j.jmb.2008.06.060;
RA Fasan R., Meharenna Y.T., Snow C.D., Poulos T.L., Arnold F.H.;
RT "Evolutionary history of a specialized p450 propane monooxygenase.";
RL J. Mol. Biol. 383:1069-1080(2008).
RN [24] {ECO:0007744|PDB:3EKB, ECO:0007744|PDB:3EKD, ECO:0007744|PDB:3EKF}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-471 OF MUTANTS CYS/MET/GLN-265
RP IN COMPLEXES WITH HEME AND PALMITOLEIC ACID, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SPECTROSCOPIC STUDIES, REDOX
RP POTENTIOMETRY OF HEME, AND MUTAGENESIS OF ALA-265.
RX PubMed=18721129; DOI=10.1042/bj20081133;
RA Girvan H.M., Toogood H.S., Littleford R.E., Seward H.E., Smith W.E.,
RA Ekanem I.S., Leys D., Cheesman M.R., Munro A.W.;
RT "Novel haem co-ordination variants of flavocytochrome P450BM3.";
RL Biochem. J. 417:65-76(2009).
RN [25] {ECO:0007744|PDB:3HF2}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-482 OF MUTANT PRO-402 IN COMPLEX
RP WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, REDOX POTENTIOMETRY OF HEME, BIOTECHNOLOGY, AND MUTAGENESIS OF
RP ILE-402.
RX PubMed=19492389; DOI=10.1002/cbic.200900279;
RA Whitehouse C.J., Bell S.G., Yang W., Yorke J.A., Blanford C.F.,
RA Strong A.J., Morse E.J., Bartlam M., Rao Z., Wong L.L.;
RT "A highly active single-mutation variant of P450BM3 (CYP102A1).";
RL ChemBioChem 10:1654-1656(2009).
RN [26] {ECO:0007744|PDB:3KX3, ECO:0007744|PDB:3KX4, ECO:0007744|PDB:3KX5}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-471 OF MUTANTS GLU-87; GLU-262
RP AND GLU-402 IN COMPLEXES WITH HEME AND N-PALMITOYLGLYCINE, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, REDOX
RP POTENTIOMETRY OF HEME, AND MUTAGENESIS OF LEU-87; PHE-262 AND ILE-402.
RX PubMed=20180779; DOI=10.1042/bj20091603;
RA Girvan H.M., Levy C.W., Williams P., Fisher K., Cheesman M.R., Rigby S.E.,
RA Leys D., Munro A.W.;
RT "Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450
RT BM3: characterization of glutamate substitution mutants at the haem site of
RT P450 BM3.";
RL Biochem. J. 427:455-466(2010).
RN [27] {ECO:0007744|PDB:3M4V}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-482 OF MUTANT PRO-331 IN COMPLEX
RP WITH HEME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, REDOX POTENTIOMETRY OF HEME, BIOTECHNOLOGY, AND MUTAGENESIS OF
RP ALA-331.
RX PubMed=21110374; DOI=10.1002/cbic.201000421;
RA Whitehouse C.J., Yang W., Yorke J.A., Rowlatt B.C., Strong A.J.,
RA Blanford C.F., Bell S.G., Bartlam M., Wong L.L., Rao Z.;
RT "Structural basis for the properties of two single-site proline mutants of
RT CYP102A1 (P450BM3).";
RL ChemBioChem 11:2549-2556(2010).
RN [28] {ECO:0007744|PDB:3NPL}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-464 OF MUTANT
RP ALA-63/CYS-98/CYS-157 IN COMPLEX WITH HEME, AND REACTION MECHANISM.
RX PubMed=20947800; DOI=10.1073/pnas.1012381107;
RA Ener M.E., Lee Y.T., Winkler J.R., Gray H.B., Cheruzel L.;
RT "Photooxidation of cytochrome P450-BM3.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18783-18786(2010).
RN [29] {ECO:0007744|PDB:1ZO4, ECO:0007744|PDB:1ZOA}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-471 IN COMPLEXES WITH HEME AND
RP N-PALMITOYLGLYCINE, FUNCTION, CATALYTIC ACTIVITY, ENZYME KINETICS, AND
RP MUTAGENESIS OF ALA-329.
RX PubMed=21875028; DOI=10.1021/bi201099j;
RA Haines D.C., Hegde A., Chen B., Zhao W., Bondlela M., Humphreys J.M.,
RA Mullin D.A., Tomchick D.R., Machius M., Peterson J.A.;
RT "A single active-site mutation of P450BM-3 dramatically enhances substrate
RT binding and rate of product formation.";
RL Biochemistry 50:8333-8341(2011).
CC -!- FUNCTION: Functions as a fatty acid monooxygenase (PubMed:3106359,
CC PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892,
CC PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084,
CC PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129,
CC PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028).
CC Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3
CC positions (PubMed:1727637, PubMed:21875028). Shows activity toward
CC medium and long-chain fatty acids, with optimum chain lengths of 12, 14
CC and 16 carbons (lauric, myristic, and palmitic acids). Able to
CC metabolize some of these primary metabolites to secondary and tertiary
CC products (PubMed:1727637). Marginal activity towards short chain
CC lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates
CC highly branched fatty acids, which play an essential role in membrane
CC fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent
CC reductase activity in the C-terminal domain, which allows electron
CC transfer from NADPH to the heme iron of the cytochrome P450 N-terminal
CC domain (PubMed:3106359, PubMed:1727637, PubMed:16566047,
CC PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573,
CC PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086,
CC PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779,
CC PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum
CC sensing signals of other competing bacteria by oxidazing efficiently
CC acyl homoserine lactones (AHLs), molecules involved in quorum sensing
CC signaling pathways, and their lactonolysis products acyl homoserines
CC (AHs) (PubMed:18020460). {ECO:0000269|PubMed:11695892,
CC ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573,
CC ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084,
CC ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686,
CC ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460,
CC ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466,
CC ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
CC ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374,
CC ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359,
CC ECO:0000269|PubMed:7578081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:11695889,
CC ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735,
CC ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:16566047,
CC ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:1727637,
CC ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886,
CC ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:18298086,
CC ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129,
CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779,
CC ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028,
CC ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892,
CC ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573,
CC ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084,
CC ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686,
CC ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460,
CC ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466,
CC ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
CC ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374,
CC ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359,
CC ECO:0000269|PubMed:7578081};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:7578081};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10051560};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:18721129,
CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779,
CC ECO:0000269|PubMed:21110374};
CC -!- ACTIVITY REGULATION: Inhibited by N-(12-imidazolyl-dodecanoyl)-L-
CC leucine. {ECO:0000269|PubMed:18298086}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=250 uM for lauric acid at pH 7.4 at room temperature
CC {ECO:0000269|PubMed:18020460};
CC KM=34 uM for N-beta-oxolauroyl-DL-homoserine lactone
CC {ECO:0000269|PubMed:18020460};
CC KM=210 uM for N-beta-oxolauroyl-DL-homoserine
CC {ECO:0000269|PubMed:18020460};
CC KM=140 uM for N-lauroyl-DL-homoserine {ECO:0000269|PubMed:18020460};
CC KM=322 uM for lauric acid at pH 7.5 and 15 degrees Celsius
CC {ECO:0000269|PubMed:16403573};
CC KM=265 uM for lauric acid {ECO:0000269|PubMed:17868686};
CC KM=16 mM for indole {ECO:0000269|PubMed:17868686};
CC KM=87.4 uM for laurate/dodecanoate at pH 7.0 and 25 degrees Celsius
CC {ECO:0000269|PubMed:18721129};
CC KM=230 uM for lauric acid at pH 7.4 {ECO:0000269|PubMed:19492389};
CC KM=87.4 uM for laurate/dodecanoate at 25 degrees Celsius
CC {ECO:0000269|PubMed:20180779};
CC KM=5.1 uM for arachidonate at 25 degrees Celsius
CC {ECO:0000269|PubMed:20180779};
CC KM=42.4 uM for palmitic acid at pH 7.4 and 30 degrees Celsius
CC {ECO:0000269|PubMed:21110374};
CC Note=kcat is 84.1 sec(-1) for lauric acid (PubMed:16403573). kcat is
CC 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-
CC palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine.
CC kcat is 610 min(-1) for N-palmitoyl-L-glutamine. kcat is 485 min(-1)
CC for N-palmitoyl-L-glutamic acid. kcat is 1160 min(-1) for N-
CC palmitoyl-L-leucine (PubMed:18004886). kcat is 28 sec(-1) for lauric
CC acid (PubMed:17868686). kcat is 2770 min(-1) for laurate/dodecanoate
CC (PubMed:18721129). kcat is 77 for lauric acid (PubMed:19492389). kcat
CC is 2770 min(-1) for laurate/dodecanoate (PubMed:20180779). kcat is
CC 16400 min(-1) for arachidonate (PubMed:20180779). kcat is 91.4 for
CC palmitic acid (PubMed:21110374). {ECO:0000269|PubMed:16403573,
CC ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886,
CC ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
CC ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374};
CC -!- INTERACTION:
CC P14779; P14779: cyp102A1; NbExp=2; IntAct=EBI-7701704, EBI-7701704;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By pentobarbital (PubMed:1544926, PubMed:3106359).
CC Expression is negatively regulated by repressor bm3R1 at the
CC transcriptional level (PubMed:1544926). {ECO:0000269|PubMed:1544926,
CC ECO:0000269|PubMed:3106359}.
CC -!- BIOTECHNOLOGY: This protein is a target of protein engineering. Its
CC selectivity-directing and activity-enhancing mutations have been
CC extensively studied and the designed mutations allow this enzyme to act
CC on non-native substrates and/or in order to enhance production of
CC synthetically desirable end-products. {ECO:0000269|PubMed:18619466,
CC ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:21110374, ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; J04832; AAA87602.1; -; Genomic_DNA.
DR EMBL; CP009920; AJI21949.1; -; Genomic_DNA.
DR EMBL; S87512; AAK19020.1; -; Genomic_DNA.
DR PIR; A34286; A34286.
DR RefSeq; WP_034650526.1; NZ_CP035094.1.
DR PDB; 1BU7; X-ray; 1.65 A; A/B=2-456.
DR PDB; 1BVY; X-ray; 2.03 A; A/B=2-459, F=460-650.
DR PDB; 1FAG; X-ray; 2.70 A; A/B/C/D=2-472.
DR PDB; 1FAH; X-ray; 2.30 A; A/B=2-472.
DR PDB; 1JME; X-ray; 2.00 A; A/B=2-456.
DR PDB; 1JPZ; X-ray; 1.65 A; A/B=2-471.
DR PDB; 1P0V; X-ray; 2.05 A; A/B=2-456.
DR PDB; 1P0W; X-ray; 2.00 A; A/B=2-456.
DR PDB; 1P0X; X-ray; 2.00 A; A/B=2-456.
DR PDB; 1SMI; X-ray; 2.00 A; A/B=2-472.
DR PDB; 1SMJ; X-ray; 2.75 A; A/B/C/D=2-472.
DR PDB; 1YQO; X-ray; 1.90 A; A/B=2-456.
DR PDB; 1YQP; X-ray; 1.80 A; A/B=2-456.
DR PDB; 1ZO4; X-ray; 1.46 A; A/B=2-471.
DR PDB; 1ZO9; X-ray; 1.70 A; A/B=2-471.
DR PDB; 1ZOA; X-ray; 1.74 A; A/B=2-471.
DR PDB; 2BMH; X-ray; 2.00 A; A/B=2-456.
DR PDB; 2HPD; X-ray; 2.00 A; A/B=2-472.
DR PDB; 2IJ2; X-ray; 1.20 A; A/B=2-471.
DR PDB; 2IJ3; X-ray; 1.90 A; A/B=2-471.
DR PDB; 2IJ4; X-ray; 2.40 A; A/B=2-471.
DR PDB; 2J1M; X-ray; 1.70 A; A/B=2-456.
DR PDB; 2J4S; X-ray; 2.10 A; A/B=2-456.
DR PDB; 2NNB; X-ray; 1.90 A; A/B=2-472.
DR PDB; 2UWH; X-ray; 2.80 A; A/B/C/D/E/F=2-459.
DR PDB; 2X7Y; X-ray; 2.10 A; A/B=2-456.
DR PDB; 2X80; X-ray; 2.30 A; A/B=2-456.
DR PDB; 3BEN; X-ray; 1.65 A; A/B=1-470.
DR PDB; 3CBD; X-ray; 2.65 A; A/B=2-456.
DR PDB; 3DGI; X-ray; 1.95 A; A/B=2-456.
DR PDB; 3EKB; X-ray; 2.30 A; A/B=2-471.
DR PDB; 3EKD; X-ray; 2.50 A; A/B=2-471.
DR PDB; 3EKF; X-ray; 2.10 A; A/B=2-471.
DR PDB; 3HF2; X-ray; 2.20 A; A/B=1-482.
DR PDB; 3KX3; X-ray; 1.80 A; A/B=2-471.
DR PDB; 3KX4; X-ray; 1.95 A; A/B=2-471.
DR PDB; 3KX5; X-ray; 1.69 A; A/B=2-471.
DR PDB; 3M4V; X-ray; 1.90 A; A/B=1-482.
DR PDB; 3NPL; X-ray; 2.40 A; A/B=1-464.
DR PDB; 3PSX; X-ray; 1.90 A; A/B=1-482.
DR PDB; 3WSP; X-ray; 1.80 A; A/B=1-456.
DR PDB; 4DQK; X-ray; 2.40 A; A/B=659-1049.
DR PDB; 4DQL; X-ray; 2.15 A; A/B=657-1049.
DR PDB; 4DTW; X-ray; 1.80 A; A/B=2-464.
DR PDB; 4DTY; X-ray; 1.45 A; A/B=2-464.
DR PDB; 4DTZ; X-ray; 1.55 A; A/B=2-464.
DR PDB; 4DU2; X-ray; 1.90 A; A/B=1-464.
DR PDB; 4DUA; X-ray; 2.00 A; A/B=2-464.
DR PDB; 4DUB; X-ray; 1.70 A; A/B=1-464.
DR PDB; 4DUC; X-ray; 1.92 A; A/B=1-464.
DR PDB; 4DUD; X-ray; 1.85 A; A/B=2-464.
DR PDB; 4DUE; X-ray; 1.70 A; A/B=2-464.
DR PDB; 4DUF; X-ray; 1.80 A; A/B/C/D=2-464.
DR PDB; 4H23; X-ray; 3.30 A; A/B=1-464.
DR PDB; 4H24; X-ray; 2.50 A; A/B/C/D=1-464.
DR PDB; 4HGF; X-ray; 1.70 A; A/B=2-456.
DR PDB; 4HGG; X-ray; 1.70 A; A/B=2-456.
DR PDB; 4HGH; X-ray; 1.40 A; A/B=2-456.
DR PDB; 4HGI; X-ray; 1.50 A; A/B=2-456.
DR PDB; 4HGJ; X-ray; 1.90 A; A/B=2-456.
DR PDB; 4KEW; X-ray; 1.89 A; A/B=2-456.
DR PDB; 4KEY; X-ray; 2.05 A; A/B=2-456.
DR PDB; 4KF0; X-ray; 1.45 A; A/B=2-458.
DR PDB; 4KF2; X-ray; 1.82 A; A/B=2-458.
DR PDB; 4KPA; X-ray; 2.00 A; A=1-471.
DR PDB; 4KPB; X-ray; 2.10 A; A/B=1-471.
DR PDB; 4O4P; X-ray; 1.83 A; A/B=2-456.
DR PDB; 4RSN; X-ray; 2.70 A; A/B=1-456.
DR PDB; 4WG2; X-ray; 2.66 A; A/B/C=2-464.
DR PDB; 4ZF6; X-ray; 2.77 A; A=1-461.
DR PDB; 4ZF8; X-ray; 2.77 A; A=1-461.
DR PDB; 4ZFA; X-ray; 2.77 A; A=1-461.
DR PDB; 4ZFB; X-ray; 2.84 A; A=1-461.
DR PDB; 5B2U; X-ray; 1.90 A; A/B=1-456.
DR PDB; 5B2V; X-ray; 2.30 A; A/B=1-456.
DR PDB; 5B2W; X-ray; 1.65 A; A/B=1-456.
DR PDB; 5B2X; X-ray; 1.90 A; A/B=1-456.
DR PDB; 5B2Y; X-ray; 2.01 A; A/B=1-456.
DR PDB; 5DYP; X-ray; 2.40 A; A/C=2-471.
DR PDB; 5DYZ; X-ray; 1.97 A; A/C=2-471.
DR PDB; 5E78; X-ray; 2.00 A; A/B=2-456.
DR PDB; 5E7Y; X-ray; 2.00 A; A/B=2-472.
DR PDB; 5E9Z; X-ray; 2.23 A; A/B/C/D=1-468.
DR PDB; 5JQ2; X-ray; 2.00 A; A/B=2-464.
DR PDB; 5JQU; X-ray; 2.16 A; A/B/C/D/E/F/G/H=2-464.
DR PDB; 5JQV; X-ray; 2.34 A; A/B/C/D/E/F/G/H=2-464.
DR PDB; 5JTD; X-ray; 1.50 A; A/B=2-464.
DR PDB; 5OG9; X-ray; 2.09 A; A/B=2-474.
DR PDB; 5UCW; X-ray; 1.70 A; A/B=1-464.
DR PDB; 5XA3; X-ray; 2.20 A; A/B/C/D=1-456.
DR PDB; 5XHJ; X-ray; 2.00 A; A/B=1-456.
DR PDB; 5ZIS; X-ray; 3.10 A; A/B/C/D=2-456.
DR PDB; 5ZLH; X-ray; 3.40 A; A/B/C/D=2-456.
DR PDB; 6H1O; X-ray; 1.73 A; A/B=2-458.
DR PDB; 6H1S; X-ray; 1.95 A; A/B=2-458.
DR PDB; 6HN8; X-ray; 2.00 A; A/B=1-456.
DR PDB; 6IAO; X-ray; 2.16 A; A/B/C/D=1-473.
DR PDB; 6JLV; X-ray; 1.22 A; A/B=1-456.
DR PDB; 6JMH; X-ray; 1.46 A; A/B=1-456.
DR PDB; 6JMW; X-ray; 1.85 A; A/B=1-457.
DR PDB; 6JO1; X-ray; 2.10 A; A/B=1-456.
DR PDB; 6JS8; X-ray; 1.36 A; A/B=1-456.
DR PDB; 6JVC; X-ray; 1.75 A; A/C=1-456.
DR PDB; 6JZS; X-ray; 1.68 A; A/C=1-457.
DR PDB; 6K24; X-ray; 2.10 A; A/B=2-457.
DR PDB; 6K3Q; X-ray; 2.06 A; A/B=1-456.
DR PDB; 6K58; X-ray; 1.41 A; A/B=1-456.
DR PDB; 6K9S; X-ray; 1.55 A; A/B=1-456.
DR PDB; 6L1A; X-ray; 1.84 A; A/B=1-456.
DR PDB; 6L1B; X-ray; 1.74 A; A/B=1-456.
DR PDB; 6LY4; X-ray; 1.68 A; A=3-457.
DR PDB; 7CKN; X-ray; 1.55 A; A/B=1-456.
DR PDB; 7CON; X-ray; 1.46 A; A/B=1-456.
DR PDB; 7COO; X-ray; 1.49 A; A/B=1-456.
DR PDB; 7CP8; X-ray; 1.68 A; A/B=1-456.
DR PDB; 7CVR; X-ray; 1.60 A; A/B=1-456.
DR PDB; 7CX6; X-ray; 1.69 A; A/B=1-456.
DR PDB; 7CX8; X-ray; 1.70 A; A/B=1-456.
DR PDB; 7CZI; X-ray; 1.64 A; A/B=1-456.
DR PDB; 7D0T; X-ray; 1.74 A; A/B=1-456.
DR PDB; 7D0U; X-ray; 1.68 A; A/B=1-456.
DR PDB; 7D1F; X-ray; 1.45 A; A/B=1-456.
DR PDB; 7E46; X-ray; 1.91 A; A/B=1-456.
DR PDB; 7EGN; X-ray; 2.70 A; A/B=1-456.
DR PDBsum; 1BU7; -.
DR PDBsum; 1BVY; -.
DR PDBsum; 1FAG; -.
DR PDBsum; 1FAH; -.
DR PDBsum; 1JME; -.
DR PDBsum; 1JPZ; -.
DR PDBsum; 1P0V; -.
DR PDBsum; 1P0W; -.
DR PDBsum; 1P0X; -.
DR PDBsum; 1SMI; -.
DR PDBsum; 1SMJ; -.
DR PDBsum; 1YQO; -.
DR PDBsum; 1YQP; -.
DR PDBsum; 1ZO4; -.
DR PDBsum; 1ZO9; -.
DR PDBsum; 1ZOA; -.
DR PDBsum; 2BMH; -.
DR PDBsum; 2HPD; -.
DR PDBsum; 2IJ2; -.
DR PDBsum; 2IJ3; -.
DR PDBsum; 2IJ4; -.
DR PDBsum; 2J1M; -.
DR PDBsum; 2J4S; -.
DR PDBsum; 2NNB; -.
DR PDBsum; 2UWH; -.
DR PDBsum; 2X7Y; -.
DR PDBsum; 2X80; -.
DR PDBsum; 3BEN; -.
DR PDBsum; 3CBD; -.
DR PDBsum; 3DGI; -.
DR PDBsum; 3EKB; -.
DR PDBsum; 3EKD; -.
DR PDBsum; 3EKF; -.
DR PDBsum; 3HF2; -.
DR PDBsum; 3KX3; -.
DR PDBsum; 3KX4; -.
DR PDBsum; 3KX5; -.
DR PDBsum; 3M4V; -.
DR PDBsum; 3NPL; -.
DR PDBsum; 3PSX; -.
DR PDBsum; 3WSP; -.
DR PDBsum; 4DQK; -.
DR PDBsum; 4DQL; -.
DR PDBsum; 4DTW; -.
DR PDBsum; 4DTY; -.
DR PDBsum; 4DTZ; -.
DR PDBsum; 4DU2; -.
DR PDBsum; 4DUA; -.
DR PDBsum; 4DUB; -.
DR PDBsum; 4DUC; -.
DR PDBsum; 4DUD; -.
DR PDBsum; 4DUE; -.
DR PDBsum; 4DUF; -.
DR PDBsum; 4H23; -.
DR PDBsum; 4H24; -.
DR PDBsum; 4HGF; -.
DR PDBsum; 4HGG; -.
DR PDBsum; 4HGH; -.
DR PDBsum; 4HGI; -.
DR PDBsum; 4HGJ; -.
DR PDBsum; 4KEW; -.
DR PDBsum; 4KEY; -.
DR PDBsum; 4KF0; -.
DR PDBsum; 4KF2; -.
DR PDBsum; 4KPA; -.
DR PDBsum; 4KPB; -.
DR PDBsum; 4O4P; -.
DR PDBsum; 4RSN; -.
DR PDBsum; 4WG2; -.
DR PDBsum; 4ZF6; -.
DR PDBsum; 4ZF8; -.
DR PDBsum; 4ZFA; -.
DR PDBsum; 4ZFB; -.
DR PDBsum; 5B2U; -.
DR PDBsum; 5B2V; -.
DR PDBsum; 5B2W; -.
DR PDBsum; 5B2X; -.
DR PDBsum; 5B2Y; -.
DR PDBsum; 5DYP; -.
DR PDBsum; 5DYZ; -.
DR PDBsum; 5E78; -.
DR PDBsum; 5E7Y; -.
DR PDBsum; 5E9Z; -.
DR PDBsum; 5JQ2; -.
DR PDBsum; 5JQU; -.
DR PDBsum; 5JQV; -.
DR PDBsum; 5JTD; -.
DR PDBsum; 5OG9; -.
DR PDBsum; 5UCW; -.
DR PDBsum; 5XA3; -.
DR PDBsum; 5XHJ; -.
DR PDBsum; 5ZIS; -.
DR PDBsum; 5ZLH; -.
DR PDBsum; 6H1O; -.
DR PDBsum; 6H1S; -.
DR PDBsum; 6HN8; -.
DR PDBsum; 6IAO; -.
DR PDBsum; 6JLV; -.
DR PDBsum; 6JMH; -.
DR PDBsum; 6JMW; -.
DR PDBsum; 6JO1; -.
DR PDBsum; 6JS8; -.
DR PDBsum; 6JVC; -.
DR PDBsum; 6JZS; -.
DR PDBsum; 6K24; -.
DR PDBsum; 6K3Q; -.
DR PDBsum; 6K58; -.
DR PDBsum; 6K9S; -.
DR PDBsum; 6L1A; -.
DR PDBsum; 6L1B; -.
DR PDBsum; 6LY4; -.
DR PDBsum; 7CKN; -.
DR PDBsum; 7CON; -.
DR PDBsum; 7COO; -.
DR PDBsum; 7CP8; -.
DR PDBsum; 7CVR; -.
DR PDBsum; 7CX6; -.
DR PDBsum; 7CX8; -.
DR PDBsum; 7CZI; -.
DR PDBsum; 7D0T; -.
DR PDBsum; 7D0U; -.
DR PDBsum; 7D1F; -.
DR PDBsum; 7E46; -.
DR PDBsum; 7EGN; -.
DR AlphaFoldDB; P14779; -.
DR SMR; P14779; -.
DR MINT; P14779; -.
DR BindingDB; P14779; -.
DR ChEMBL; CHEMBL4630872; -.
DR DrugBank; DB08086; N-[12-(1H-imidazol-1-yl)dodecanoyl]-L-leucine.
DR DrugBank; DB03440; N-hexadecanoylglycine.
DR DrugBank; DB04257; Palmitoleic Acid.
DR PRIDE; P14779; -.
DR EnsemblBacteria; AJI21949; AJI21949; BG04_163.
DR KEGG; bmeg:BG04_163; -.
DR HOGENOM; CLU_001570_7_0_9; -.
DR BioCyc; MetaCyc:MON-17698; -.
DR BRENDA; 1.1.1.B57; 656.
DR BRENDA; 1.14.14.1; 656.
DR BRENDA; 1.6.2.4; 656.
DR EvolutionaryTrace; P14779; -.
DR Proteomes; UP000031829; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; -; 1.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR023206; Bifunctional_P450_P450_red.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; SSF48264; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Electron transport; FAD; Flavoprotein; FMN; Heme;
KW Iron; Metal-binding; Monooxygenase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Transport.
FT CHAIN 1..1049
FT /note="Bifunctional cytochrome P450/NADPH--P450 reductase"
FT /id="PRO_0000052205"
FT DOMAIN 483..622
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 660..892
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 2..472
FT /note="Cytochrome P450"
FT REGION 473..1049
FT /note="NADPH--P450 reductase"
FT BINDING 52
FT /ligand="(9Z)-hexadecenoate"
FT /ligand_id="ChEBI:CHEBI:32372"
FT /evidence="ECO:0000269|PubMed:15020590,
FT ECO:0007744|PDB:1SMJ"
FT BINDING 401
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:10051560,
FT ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892,
FT ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:15020590,
FT ECO:0000269|PubMed:15299332, ECO:0000269|PubMed:16403573,
FT ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:17429965,
FT ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886,
FT ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466,
FT ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389,
FT ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:20947800,
FT ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028,
FT ECO:0000269|PubMed:7578081, ECO:0000269|PubMed:8342039,
FT ECO:0000269|PubMed:9033595, ECO:0007744|PDB:1BU7,
FT ECO:0007744|PDB:1BVY, ECO:0007744|PDB:1FAG,
FT ECO:0007744|PDB:1FAH, ECO:0007744|PDB:1JME,
FT ECO:0007744|PDB:1JPZ, ECO:0007744|PDB:1P0V,
FT ECO:0007744|PDB:1P0W, ECO:0007744|PDB:1P0X,
FT ECO:0007744|PDB:1SMI, ECO:0007744|PDB:1SMJ,
FT ECO:0007744|PDB:1YQO, ECO:0007744|PDB:1YQP,
FT ECO:0007744|PDB:1ZO4, ECO:0007744|PDB:1ZO9,
FT ECO:0007744|PDB:1ZOA, ECO:0007744|PDB:2BMH,
FT ECO:0007744|PDB:2HPD, ECO:0007744|PDB:2IJ2,
FT ECO:0007744|PDB:2IJ3, ECO:0007744|PDB:2IJ4,
FT ECO:0007744|PDB:2J1M, ECO:0007744|PDB:2J4S,
FT ECO:0007744|PDB:2UWH, ECO:0007744|PDB:3BEN,
FT ECO:0007744|PDB:3CBD, ECO:0007744|PDB:3EKB,
FT ECO:0007744|PDB:3EKD, ECO:0007744|PDB:3EKF,
FT ECO:0007744|PDB:3HF2, ECO:0007744|PDB:3KX3,
FT ECO:0007744|PDB:3KX4, ECO:0007744|PDB:3KX5,
FT ECO:0007744|PDB:3M4V, ECO:0007744|PDB:3NPL"
FT BINDING 489..494
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10051560,
FT ECO:0007744|PDB:1BVY"
FT BINDING 536..539
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10051560,
FT ECO:0007744|PDB:1BVY"
FT BINDING 570..572
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10051560,
FT ECO:0007744|PDB:1BVY"
FT BINDING 578..580
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:10051560,
FT ECO:0007744|PDB:1BVY"
FT SITE 269
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:16403573,
FT ECO:0000305|PubMed:7578081"
FT MUTAGEN 48
FT /note="R->Q,S: 2-3-fold decrease in binding affinity for N-
FT myristoyl-L-methionine as substrate."
FT /evidence="ECO:0000269|PubMed:18004886"
FT MUTAGEN 75
FT /note="A->G: Higher activity in the hydroxylation of highly
FT branched fatty acids; when associated with V-88 and Q-189."
FT /evidence="ECO:0000269|PubMed:16566047"
FT MUTAGEN 83
FT /note="A->F: 800-fold binding affinity for laurate as
FT substrate. High coupling of NADPH consumption to laurate
FT formation. Very much more effective in indole
FT hydroxylation. Favors omega-2 hydroxylation. Significantly
FT higher rates of NADPH consumption in the absence of
FT substrate. No temperature-dependent shifts to low-spin in
FT complex with palmitate."
FT /evidence="ECO:0000269|PubMed:17868686"
FT MUTAGEN 83
FT /note="A->I: No effect in binding affinity for laurate as
FT substrate. High coupling of NADPH consumption to laurate
FT formation. No indole hydroxylation. Favors omega-2
FT hydroxylation. Similarly to wild-type, shows significant
FT shifts to low-spin in complex with palmitate as the
FT temperature decreases."
FT /evidence="ECO:0000269|PubMed:17868686"
FT MUTAGEN 83
FT /note="A->W: 800-fold binding affinity for laurate as
FT substrate. Low coupling of NADPH consumption to laurate
FT formation. Very much more effective in indole
FT hydroxylation. Favors omega-1 hydroxylation. Significantly
FT higher rates of NADPH consumption in the absence of
FT substrate. No temperature-dependent shifts to low-spin in
FT complex with palmitate."
FT /evidence="ECO:0000269|PubMed:17868686"
FT MUTAGEN 87
FT /note="L->E: Ineffective covalent modification of the heme
FT macrocycle. Extensive formation of Fe(II)CO complex in the
FT substrate-free form. Has more positive potential in both
FT substrate-free and arachidonate-bound forms and some high-
FT spin content in the ferric substrate-free form of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:20180779"
FT MUTAGEN 88
FT /note="F->V: Higher activity in the hydroxylation of highly
FT branched fatty acids; when associated with G-75 and Q-189."
FT /evidence="ECO:0000269|PubMed:16566047"
FT MUTAGEN 189
FT /note="L->Q: Higher activity in the hydroxylation of highly
FT branched fatty acids; when associated with G-75 and V-88."
FT /evidence="ECO:0000269|PubMed:16566047"
FT MUTAGEN 262
FT /note="F->E: Ineffective covalent modification of the heme
FT macrocycle. Substantially slower FMN to heme electron
FT transfer for the arachidonate-bound enzyme. Product
FT distribution biased towards omega-3."
FT /evidence="ECO:0000269|PubMed:20180779"
FT MUTAGEN 265
FT /note="A->C: No effective fatty acid oxidation. No effect
FT on electron transport from NADPH to FMN. Substantially
FT lower high-spin conversion with arachidonate and
FT palmitoleate, and negligible change is observed with
FT palmitate, myristate and laurate/dodecanoate. 20% of omega-
FT 1, omega-2 and omega-3 laurate/dodecanoate hydroxylation
FT products."
FT /evidence="ECO:0000269|PubMed:18721129"
FT MUTAGEN 265
FT /note="A->H,K: No significant stimulation of NADPH
FT oxidation induced by addition of fatty acids and no
FT hydroxylated products, but cytochrome c reductase activity
FT levels are identical to wild-type enzyme. More negative
FT reduction potential with dithionite. Unable to form
FT Fe(2+)CO complexes on reduction with dithionite and
FT bubbling with carbon monoxide."
FT /evidence="ECO:0000269|PubMed:17077084"
FT MUTAGEN 265
FT /note="A->M: No effective fatty acid oxidation. No effect
FT on electron transport from NADPH to FMN. Slightly lower
FT high-spin conversion with arachidonate, palmitoleate,
FT palmitate, myristate and laurate/dodecanoate. 5% of omega-
FT 1, omega-2 and omega-3 laurate/dodecanoate hydroxylation
FT products."
FT /evidence="ECO:0000269|PubMed:18721129"
FT MUTAGEN 265
FT /note="A->Q: No effective fatty acid oxidation. No effect
FT on electron transport from NADPH to FMN. Nearly wild-type
FT level of high-spin conversion with laurate/dodecanoate,
FT palmitoleate and arachidonate. 5% of omega-1, omega-2 and
FT omega-3 laurate/dodecanoate hydroxylation products."
FT /evidence="ECO:0000269|PubMed:18721129"
FT MUTAGEN 269
FT /note="T->A: Contrary to wild-type, significant decrease in
FT the formation of the high-spin complex via substrate
FT binding, and decreased substrate-induced reduction
FT potential shift with saturating concentrations of
FT arachidonate; when associated with H-394. Considerably
FT lower proportion of high-spin protein and decreased
FT substrate-induced heme reduction-potential shift on
FT addition of saturating concentrations of arachidonate.
FT Leads to destabilization of the oxy-ferrous complex.
FT Exhibits slower rates of O(2) and NADPH consumption using
FT sodium laurate as the substrate. Greater production of
FT water and peroxide compared to wild-type indicating
FT uncoupled electron transfer from sodium laurate
FT hydroxylation. Only 16% yield of product after 5 min of
FT reaction relative to the amount of NADPH used compared to
FT 100% of wild-type."
FT /evidence="ECO:0000269|PubMed:16403573,
FT ECO:0000269|PubMed:7578081"
FT MUTAGEN 269
FT /note="T->N: High substrate-free turnover rate constant.
FT Negligible substrate-induced spin-state and substrate-
FT induced heme reduction-potential shifts on addition of
FT saturating concentrations of arachidonate. Induces a
FT positive shift in the substrate-free heme reduction
FT potential. 10-fold greater rate constants for the first
FT electron transfer in the absence of substrate; when
FT associated with H-394. Turnover rate constants diminished.
FT Significantly smaller degrees of coupling to product.
FT Negligible amounts of high-spin protein on addition of
FT saturating concentration of arachidonate. Negligible
FT substrate-induced spin-state and substrate-induced heme
FT reduction-potential shifts on addition of saturating
FT concentrations of arachidonate. Induces a 60 mV positive
FT shift in the substrate-free heme reduction potential. The
FT apparent rate constant for heme reduction is smaller than
FT the overall turnover rate constant. Leads to
FT destabilization of the oxy-ferrous complex."
FT /evidence="ECO:0000269|PubMed:16403573"
FT MUTAGEN 329
FT /note="A->V: Substrate binding affinity increases 5-10 fold
FT and the turnover number increases 2-8-fold for palmitate as
FT substrate compared to the wild-type. Has a very different
FT product distribution favoring greatly oxidation at the
FT omega-1 position and shows almost no oxidation at the
FT omega-3 position."
FT /evidence="ECO:0000269|PubMed:21875028"
FT MUTAGEN 331
FT /note="A->P: Enhanced activity with small non-natural
FT substrates with altered product profiles compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:21110374"
FT MUTAGEN 394
FT /note="F->H: High substrate-free turnover rate constant.
FT Negligible substrate-induced spin-state and substrate-
FT induced heme reduction-potential shifts on addition of
FT saturating concentrations of arachidonate. Induces a
FT positive shift in the substrate-free heme reduction
FT potential. 10-fold greater rate constants for the first
FT electron transfer in the absence of substrate; when
FT associated with N-269. Significant decrease in the
FT formation of the high-spin complex via substrate binding,
FT and decreased substrate-induced reduction potential shift
FT with saturating concentrations of arachidonate; when
FT associated with A-269. No change in product profile using
FT myristate as substrate, but slightly higher amount of
FT unreacted myristate indicating lower overall catalytic
FT activity relative to wild-type."
FT /evidence="ECO:0000269|PubMed:11695889,
FT ECO:0000269|PubMed:16403573"
FT MUTAGEN 394
FT /note="F->W: Large decrease in the heme reduction potential
FT in the presence and absence of substrate arachidonate. 10%
FT reduction in efficiency to couple NADPH consumption to
FT substrate monooxygenation. Half of the turn over rate and
FT four times faster decay of the oxy-ferrous complex to the
FT ferric form than that of wild-type."
FT /evidence="ECO:0000269|PubMed:14653735"
FT MUTAGEN 402
FT /note="I->E: Ineffective covalent modification of the heme
FT macrocycle. 2-fold apparent limiting rate of flavin to heme
FT electron transfer for arachidonate-bound enzyme. Substrate-
FT free enzyme is converted rapidly and completely into its
FT Fe(II)CO complex and has much more positive potential. 8-
FT fold decrease in overall catalytic rate with arachidonic
FT acid. More efficient NADPH oxidase in absence of fatty
FT acids. Product distribution biased towards omega-1."
FT /evidence="ECO:0000269|PubMed:20180779"
FT MUTAGEN 402
FT /note="I->P: 10-fold increase in binding affinity for
FT lauric acid. Catalytic activity rates accelerate across a
FT range of hydrophobic non-natural substrates, including (+)-
FT alpha-pinene, fluorene, 3-methylpentane and propylbenzene,
FT while product distributions of them are broadly similar to
FT the wild-type enzyme exept for (+)-alpha-pinene which is
FT not metabolized by wild-type."
FT /evidence="ECO:0000269|PubMed:19492389"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6K24"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:2IJ2"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5JQU"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2IJ2"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 113..132
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5JQV"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6JLV"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4HGJ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 200..227
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:2IJ2"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 252..283
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2IJ2"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:2IJ2"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:6JLV"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4ZFB"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 404..421
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 434..442
FT /evidence="ECO:0007829|PDB:2IJ2"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:2IJ2"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:4WG2"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:1BVY"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:1BVY"
FT HELIX 493..506
FT /evidence="ECO:0007829|PDB:1BVY"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:1BVY"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:1BVY"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:1BVY"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:1BVY"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:1BVY"
FT HELIX 546..553
FT /evidence="ECO:0007829|PDB:1BVY"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:1BVY"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:1BVY"
FT HELIX 581..591
FT /evidence="ECO:0007829|PDB:1BVY"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:1BVY"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:1BVY"
FT HELIX 610..628
FT /evidence="ECO:0007829|PDB:1BVY"
FT STRAND 663..672
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 682..688
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 709..719
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 726..729
FT /evidence="ECO:0007829|PDB:4DQK"
FT STRAND 741..746
FT /evidence="ECO:0007829|PDB:4DQK"
FT HELIX 747..750
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 751..753
FT /evidence="ECO:0007829|PDB:4DQK"
FT STRAND 756..759
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 762..770
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 775..783
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 787..793
FT /evidence="ECO:0007829|PDB:4DQL"
FT TURN 794..798
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 801..807
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 815..820
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:4DQL"
FT TURN 836..838
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 842..848
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 864..871
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 877..883
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 899..902
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 905..908
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 909..923
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 931..938
FT /evidence="ECO:0007829|PDB:4DQL"
FT TURN 940..942
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 947..955
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 960..967
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 976..982
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 984..992
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 996..1002
FT /evidence="ECO:0007829|PDB:4DQL"
FT TURN 1003..1005
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 1006..1022
FT /evidence="ECO:0007829|PDB:4DQL"
FT HELIX 1026..1038
FT /evidence="ECO:0007829|PDB:4DQL"
FT STRAND 1042..1047
FT /evidence="ECO:0007829|PDB:4DQL"
SQ SEQUENCE 1049 AA; 117781 MW; B0BE61F8A2EE33D5 CRC64;
MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT RYLSSQRLIK
EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA HNILLPSFSQ QAMKGYHAMM
VDIAVQLVQK WERLNADEHI EVPEDMTRLT LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR
ALDEAMNKLQ RANPDDPAYD ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN
GKDPETGEPL DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV
DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK GDELMVLIPQ
LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA CIGQQFALHE ATLVLGMMLK
HFDFEDHTNY ELDIKETLTL KPEGFVVKAK SKKIPLGGIP SPSTEQSAKK VRKKAENAHN
TPLLVLYGSN MGTAEGTARD LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH
PPDNAKQFVD WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD
RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS AADMPLAKMH
GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH LGVIPRNYEG IVNRVTARFG
LDASQQIRLE AEEEKLAHLP LAKTVSVEEL LQYVELQDPV TRTQLRAMAA KTVCPPHKVE
LEALLEKQAY KEQVLAKRLT MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE
KQASITVSVV SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI
MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL ENAQSEGIIT
LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC GDGSQMAPAV EATLMKSYAD
VHQVSEADAR LWLQQLEEKG RYAKDVWAG
