FADB_ECOLI
ID FADB_ECOLI Reviewed; 729 AA.
AC P21177; Q2M8E9;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01621};
DE Includes:
DE RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01621};
DE EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621};
DE EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621};
DE EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621};
DE Includes:
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621};
DE EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621};
GN Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; Synonyms=oldB;
GN OrderedLocusNames=b3846, JW3822;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1699931; DOI=10.1128/jb.172.11.6459-6468.1990;
RA Dirusso C.C.;
RT "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty
RT acid-oxidizing multienzyme complex, indicates a high degree of homology to
RT eucaryotic enzymes.";
RL J. Bacteriol. 172:6459-6468(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=2191949; DOI=10.1016/s0021-9258(18)86963-0;
RA Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.;
RT "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-
RT coenzyme A thiolase from Escherichia coli and the structural organization
RT of the fadAB operon.";
RL J. Biol. Chem. 265:10424-10429(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2204034; DOI=10.1093/nar/18.16.4937;
RA Nakahigashi K., Inokuchi H.;
RT "Nucleotide sequence of the fadA and fadB genes from Escherichia coli.";
RL Nucleic Acids Res. 18:4937-4937(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1712230; DOI=10.1021/bi00241a023;
RA Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y.;
RT "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and
RT primary structure of the multifunctional fatty acid oxidation protein from
RT Escherichia coli.";
RL Biochemistry 30:6788-6795(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=368024; DOI=10.1128/jb.137.1.469-473.1979;
RA Pramanik A., Pawar S., Antonian E., Schulz H.;
RT "Five different enzymatic activities are associated with the multienzyme
RT complex of fatty acid oxidation from Escherichia coli.";
RL J. Bacteriol. 137:469-473(1979).
RN [9]
RP FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1748662; DOI=10.1016/s0021-9258(18)54369-6;
RA Smeland T.E., Cuebas D., Schulz H.;
RT "Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a
RT dehydration/hydration mechanism catalyzed by the multienzyme complex of
RT fatty acid oxidation from Escherichia coli.";
RL J. Biol. Chem. 266:23904-23908(1991).
RN [10]
RP FUNCTION AS AN EPIMERASE AND HYDRATASE, CATALYTIC ACTIVITY, ACTIVE SITE,
RP MUTAGENESIS OF GLY-116, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8454629; DOI=10.1016/s0021-9258(18)53291-9;
RA Yang S.Y., Elzinga M.;
RT "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme
RT A epimerase with an active site in the amino-terminal domain of the
RT multifunctional fatty acid oxidation protein from Escherichia coli.";
RL J. Biol. Chem. 268:6588-6592(1993).
RN [11]
RP FUNCTION AS A DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, NAD-BINDING, AND MUTAGENESIS OF GLY-322 AND
RP HIS-450.
RX PubMed=8755745; DOI=10.1021/bi960374y;
RA He X.Y., Yang S.Y.;
RT "Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A
RT dehydrogenase associated with the large alpha-subunit of the multienzyme
RT complex of fatty acid oxidation from Escherichia coli.";
RL Biochemistry 35:9625-9630(1996).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x;
RA Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.;
RT "A new Escherichia coli metabolic competency: growth on fatty acids by a
RT novel anaerobic beta-oxidation pathway.";
RL Mol. Microbiol. 47:793-805(2003).
CC -!- FUNCTION: Involved in the aerobic and anaerobic degradation of long-
CC chain fatty acids via beta-oxidation cycle. Catalyzes the formation of
CC 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use
CC D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
CC {ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:12535077,
CC ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:368024,
CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53 uM for crotonyl-CoA (for enoyl-CoA hydratase activity)
CC {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629,
CC ECO:0000269|PubMed:8755745};
CC KM=8.7 mM for L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA
CC hydratase activity) {ECO:0000269|PubMed:1748662,
CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
CC KM=38 mM for D-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA
CC hydratase activity) {ECO:0000269|PubMed:1748662,
CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
CC KM=5.8 uM for 3-cis-tetradecenoyl-CoA (for Delta(3)-cis-Delta(2)-
CC trans-enoyl-CoA isomerase activity) {ECO:0000269|PubMed:1748662,
CC ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745};
CC KM=69 uM for acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase
CC activity) {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629,
CC ECO:0000269|PubMed:8755745};
CC KM=2.0 uM for NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)
CC {ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:8454629,
CC ECO:0000269|PubMed:8755745};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000255|HAMAP-Rule:MF_01621}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:368024}.
CC -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of,
CC at least, 12 carbon atoms). When LCFAs are present in the medium, they
CC are converted to long-chain acyl-CoAs which bind to FadR resulting in
CC its release from the DNA and thus derepression of the transcription.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01621}.
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DR EMBL; M59368; AAA23750.1; -; Genomic_DNA.
DR EMBL; X52837; CAB40809.1; -; Genomic_DNA.
DR EMBL; M74164; AAA62777.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67643.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76849.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77457.1; -; Genomic_DNA.
DR PIR; A39592; A39592.
DR RefSeq; NP_418288.1; NC_000913.3.
DR RefSeq; WP_000965936.1; NZ_SSZK01000046.1.
DR PDB; 6TNM; X-ray; 2.95 A; A=1-729.
DR PDBsum; 6TNM; -.
DR AlphaFoldDB; P21177; -.
DR SASBDB; P21177; -.
DR SMR; P21177; -.
DR BioGRID; 4263448; 158.
DR ComplexPortal; CPX-3964; fadBA fatty acid oxidation complex, aerobic conditions.
DR DIP; DIP-9560N; -.
DR IntAct; P21177; 7.
DR STRING; 511145.b3846; -.
DR jPOST; P21177; -.
DR PaxDb; P21177; -.
DR PRIDE; P21177; -.
DR EnsemblBacteria; AAC76849; AAC76849; b3846.
DR EnsemblBacteria; BAE77457; BAE77457; BAE77457.
DR GeneID; 948336; -.
DR KEGG; ecj:JW3822; -.
DR KEGG; eco:b3846; -.
DR PATRIC; fig|511145.12.peg.3960; -.
DR EchoBASE; EB0275; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_6; -.
DR InParanoid; P21177; -.
DR OMA; TGAGWPF; -.
DR PhylomeDB; P21177; -.
DR BioCyc; EcoCyc:FADB-MON; -.
DR BioCyc; MetaCyc:FADB-MON; -.
DR SABIO-RK; P21177; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:P21177; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IDA:EcoCyc.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IDA:UniProtKB.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:ComplexPortal.
DR HAMAP; MF_01621; FadB; 1.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR012799; FadB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 2.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR02437; FadB; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Fatty acid metabolism; Isomerase;
KW Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..729
FT /note="Fatty acid oxidation complex subunit alpha"
FT /id="PRO_0000109268"
FT REGION 1..189
FT /note="Enoyl-CoA hydratase/isomerase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT REGION 311..729
FT /note="3-hydroxyacyl-CoA dehydrogenase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT REGION 708..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 450
FT /note="For 3-hydroxyacyl-CoA dehydrogenase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621,
FT ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000305"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 400..402
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 407
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 429
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 453
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 500
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT BINDING 660
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT SITE 119
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT SITE 139
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT MUTAGEN 116
FT /note="G->F: Absence of both enoyl-CoA hydratase and 3-
FT hydroxyacyl-CoA epimerase activities. Delta(3)-cis-
FT Delta(2)-trans-enoyl-CoA isomerase is only slightly
FT affected."
FT /evidence="ECO:0000269|PubMed:8454629"
FT MUTAGEN 322
FT /note="G->A: 10-fold increase in KM for NADH."
FT /evidence="ECO:0000269|PubMed:8755745"
FT MUTAGEN 450
FT /note="H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA
FT dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:8755745"
FT CONFLICT 518
FT /note="A -> R (in Ref. 1; AAA23750)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="F -> L (in Ref. 3; CAB40809)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="P -> A (in Ref. 3; CAB40809)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 54..65
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 266..282
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 284..306
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 346..365
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 404..416
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 471..483
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 499..515
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 520..529
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 537..544
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 607..615
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 624..644
FT /evidence="ECO:0007829|PDB:6TNM"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 651..661
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 671..677
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:6TNM"
FT HELIX 701..706
FT /evidence="ECO:0007829|PDB:6TNM"
FT TURN 707..710
FT /evidence="ECO:0007829|PDB:6TNM"
SQ SEQUENCE 729 AA; 79594 MW; 6F1055E402F6B129 CRC64;
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG EAIGVLEQQS DLKGLLLRSN
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTIAAVN GYALGGGCEC
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK
IGLVDGVVKA EKLVEGAKAV LRQAINGDLD WKAKRQPKLE PLKLSKIEAT MSFTIAKGMV
AQTAGKHYPA PITAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK
GKAKKLTKDV ETPKQAAVLG AGIMGGGIAY QSAWKGVPVV MKDINDKSLT LGMTEAAKLL
NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDIVVEAV VENPKVKKAV LAETEQKVRQ
DTVLASNTST IPISELANAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKIDKVMEKQ FGWPMGPAYL
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP
KKEEDAAVED LLAEVSQPKR DFSEEEIIAR MMIPMVNEVV RCLEEGIIAT PAEADMALVY
GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QHLGPLYEVP EGLRNKARHN EPYYPPVEPA
RPVGDLKTA
