DXR_ECOLI
ID DXR_ECOLI Reviewed; 398 AA.
AC P45568; P77209; Q8KMY5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase;
DE Short=DXP reductoisomerase;
DE EC=1.1.1.267 {ECO:0000269|PubMed:10631325, ECO:0000269|PubMed:10787409, ECO:0000269|PubMed:9707569};
DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase;
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase;
GN Name=dxr; Synonyms=ispC, yaeM; OrderedLocusNames=b0173, JW0168;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9707569; DOI=10.1073/pnas.95.17.9879;
RA Takahashi S., Kuzuyama T., Watanabe H., Seto H.;
RT "A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation
RT of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate
RT pathway for terpenoid biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9879-9884(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 277-284.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-204.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RX PubMed=1447125; DOI=10.1128/jb.174.23.7517-7526.1992;
RA Yamanaka K., Ogura T., Niki H., Hiraga S.;
RT "Identification and characterization of the smbA gene, a suppressor of the
RT mukB null mutant of Escherichia coli.";
RL J. Bacteriol. 174:7517-7526(1992).
RN [8]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10631325; DOI=10.1016/s0014-5793(99)01743-3;
RA Radykewicz T., Rohdich F., Wungsintaweekul J., Herz S., Kis K.,
RA Eisenreich W., Bacher A., Zenk M.H., Arigoni D.;
RT "Biosynthesis of terpenoids: 1-deoxy-D-xylulose-5-phosphate
RT reductoisomerase from Escherichia coli is a class B dehydrogenase.";
RL FEBS Lett. 465:157-160(2000).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP MUTAGENESIS OF GLY-14; HIS-153; HIS-209; GLU-231 AND HIS-257.
RX PubMed=10787409; DOI=10.1074/jbc.m001820200;
RA Kuzuyama T., Takahashi S., Takagi M., Seto H.;
RT "Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an
RT enzyme involved in isopentenyl diphosphate biosynthesis, and identification
RT of its catalytic amino acid residues.";
RL J. Biol. Chem. 275:19928-19932(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-398 IN COMPLEX WITH NADPH.
RX PubMed=11872159; DOI=10.1093/oxfordjournals.jbchem.a003105;
RA Yajima S., Nonaka T., Kuzuyama T., Seto H., Ohsawa K.;
RT "Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase
RT complexed with cofactors: implications of a flexible loop movement upon
RT substrate binding.";
RL J. Biochem. 131:313-317(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=11741911; DOI=10.1074/jbc.m109500200;
RA Reuter K., Sanderbrand S., Jomaa H., Wiesner J., Steinbrecher I., Beck E.,
RA Hintz M., Klebe G., Stubbs M.T.;
RT "Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a
RT crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis.";
RL J. Biol. Chem. 277:5378-5384(2002).
RN [13] {ECO:0007744|PDB:1ONN, ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND
RP FOSMIDOMYCIN, AND SUBUNIT.
RX PubMed=12621040; DOI=10.1074/jbc.m300993200;
RA Steinbacher S., Kaiser J., Eisenreich W., Huber R., Bacher A., Rohdich F.;
RT "Structural basis of fosmidomycin action revealed by the complex with 2-C-
RT methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the
RT catalytic mechanism and anti-malaria drug development.";
RL J. Biol. Chem. 278:18401-18407(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-398 IN COMPLEX WITH SUBSTRATE
RP ANALOG.
RX PubMed=15339150; DOI=10.1021/ja040126m;
RA Yajima S., Hara K., Sanders J.M., Yin F., Ohsawa K., Wiesner J., Jomaa H.,
RA Oldfield E.;
RT "Crystallographic structures of two bisphosphonate:1-deoxyxylulose-5-
RT phosphate reductoisomerase complexes.";
RL J. Am. Chem. Soc. 126:10824-10825(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE;
RP FOSMIDOMYCIN AND NADP, AND SUBUNIT.
RX PubMed=15567415; DOI=10.1016/j.jmb.2004.10.030;
RA Mac Sweeney A., Lange R., Fernandes R.P., Schulz H., Dale G.E.,
RA Douangamath A., Proteau P.J., Oefner C.;
RT "The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate
RT reductoisomerase in a ternary complex with the antimalarial compound
RT fosmidomycin and NADPH reveals a tight-binding closed enzyme
RT conformation.";
RL J. Mol. Biol. 345:115-127(2005).
CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of
CC 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC phosphate (MEP). {ECO:0000269|PubMed:10631325,
CC ECO:0000269|PubMed:10787409, ECO:0000269|PubMed:9707569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-
CC xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267;
CC Evidence={ECO:0000269|PubMed:10631325, ECO:0000269|PubMed:10787409,
CC ECO:0000269|PubMed:9707569};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC Evidence={ECO:0000269|PubMed:10631325, ECO:0000269|PubMed:10787409,
CC ECO:0000269|PubMed:9707569};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10787409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10787409};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:10787409};
CC Note=Divalent cation. Prefers Mg(2+), Mn(2+) or Co(2+).
CC {ECO:0000269|PubMed:10787409};
CC -!- ACTIVITY REGULATION: Inhibited by fosmidomycin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=250 uM for DXP {ECO:0000269|PubMed:10787409};
CC Note=Measured in the presence of manganese ions.;
CC pH dependence:
CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:10787409};
CC Temperature dependence:
CC Optimum temperature is 40-60 degrees Celsius.
CC {ECO:0000269|PubMed:10787409};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 1/6. {ECO:0000269|PubMed:9707569}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11741911,
CC ECO:0000269|PubMed:11872159, ECO:0000269|PubMed:12621040,
CC ECO:0000269|PubMed:15339150, ECO:0000269|PubMed:15567415}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
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DR EMBL; AB013300; BAA32426.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08602.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73284.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77848.2; -; Genomic_DNA.
DR EMBL; D13334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64741; E64741.
DR RefSeq; NP_414715.1; NC_000913.3.
DR RefSeq; WP_000811923.1; NZ_SSZK01000004.1.
DR PDB; 1JVS; X-ray; 2.20 A; A/B=2-398.
DR PDB; 1K5H; X-ray; 2.50 A; A/B/C=1-398.
DR PDB; 1ONN; X-ray; 2.60 A; A/B=1-398.
DR PDB; 1ONO; X-ray; 2.50 A; A/B=1-398.
DR PDB; 1ONP; X-ray; 2.50 A; A/B=1-398.
DR PDB; 1Q0H; X-ray; 2.20 A; A=1-398.
DR PDB; 1Q0L; X-ray; 2.65 A; A=1-398.
DR PDB; 1Q0Q; X-ray; 1.90 A; A/B=1-398.
DR PDB; 1T1R; X-ray; 2.30 A; A/B=2-398.
DR PDB; 1T1S; X-ray; 2.40 A; A/B=2-398.
DR PDB; 2EGH; X-ray; 2.20 A; A/B=2-398.
DR PDB; 3ANL; X-ray; 2.10 A; A/B=2-398.
DR PDB; 3ANM; X-ray; 2.00 A; A/B=2-398.
DR PDB; 3ANN; X-ray; 2.00 A; A/B=2-398.
DR PDB; 3R0I; X-ray; 2.10 A; A/B=1-398.
DR PDBsum; 1JVS; -.
DR PDBsum; 1K5H; -.
DR PDBsum; 1ONN; -.
DR PDBsum; 1ONO; -.
DR PDBsum; 1ONP; -.
DR PDBsum; 1Q0H; -.
DR PDBsum; 1Q0L; -.
DR PDBsum; 1Q0Q; -.
DR PDBsum; 1T1R; -.
DR PDBsum; 1T1S; -.
DR PDBsum; 2EGH; -.
DR PDBsum; 3ANL; -.
DR PDBsum; 3ANM; -.
DR PDBsum; 3ANN; -.
DR PDBsum; 3R0I; -.
DR AlphaFoldDB; P45568; -.
DR SMR; P45568; -.
DR BioGRID; 4259751; 202.
DR ComplexPortal; CPX-1930; DXP reductoisomerase complex.
DR DIP; DIP-9484N; -.
DR IntAct; P45568; 6.
DR STRING; 511145.b0173; -.
DR BindingDB; P45568; -.
DR ChEMBL; CHEMBL4091; -.
DR DrugBank; DB02496; 1-Deoxy-D-xylulose 5-phosphate.
DR DrugBank; DB03649; [{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate.
DR DrugBank; DB02948; Fosmidomycin.
DR jPOST; P45568; -.
DR PaxDb; P45568; -.
DR PRIDE; P45568; -.
DR EnsemblBacteria; AAC73284; AAC73284; b0173.
DR EnsemblBacteria; BAA77848; BAA77848; BAA77848.
DR GeneID; 66671539; -.
DR GeneID; 945019; -.
DR KEGG; ecj:JW0168; -.
DR KEGG; eco:b0173; -.
DR PATRIC; fig|1411691.4.peg.2107; -.
DR EchoBASE; EB2575; -.
DR eggNOG; COG0743; Bacteria.
DR HOGENOM; CLU_035714_4_0_6; -.
DR InParanoid; P45568; -.
DR OMA; PIDSEHF; -.
DR PhylomeDB; P45568; -.
DR BioCyc; EcoCyc:DXPREDISOM-MON; -.
DR BioCyc; MetaCyc:DXPREDISOM-MON; -.
DR BRENDA; 1.1.1.267; 2026.
DR SABIO-RK; P45568; -.
DR UniPathway; UPA00056; UER00092.
DR EvolutionaryTrace; P45568; -.
DR PRO; PR:P45568; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990065; C:Dxr protein complex; IPI:ComplexPortal.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IMP:EcoCyc.
DR GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IDA:ComplexPortal.
DR HAMAP; MF_00183; DXP_reductoisom; 1.
DR InterPro; IPR003821; DXP_reductoisomerase.
DR InterPro; IPR013644; DXP_reductoisomerase_C.
DR InterPro; IPR013512; DXP_reductoisomerase_N.
DR InterPro; IPR026877; DXPR_C.
DR InterPro; IPR036169; DXPR_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR30525; PTHR30525; 1.
DR Pfam; PF08436; DXP_redisom_C; 1.
DR Pfam; PF02670; DXP_reductoisom; 1.
DR Pfam; PF13288; DXPR_C; 1.
DR PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69055; SSF69055; 1.
DR TIGRFAMs; TIGR00243; Dxr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Isoprene biosynthesis; Magnesium; Manganese;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..398
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163651"
FT REGION 222..228
FT /note="Binding to substrate phosphate group"
FT /evidence="ECO:0000269|PubMed:15567415,
FT ECO:0007744|PDB:1Q0Q"
FT BINDING 7..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11872159,
FT ECO:0000269|PubMed:15567415"
FT BINDING 125
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000269|PubMed:15567415,
FT ECO:0007744|PDB:1Q0Q"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:12621040,
FT ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP"
FT BINDING 152
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000269|PubMed:15567415,
FT ECO:0007744|PDB:1Q0Q"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:12621040,
FT ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP"
FT BINDING 186
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000269|PubMed:15567415,
FT ECO:0007744|PDB:1Q0Q"
FT BINDING 209
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000269|PubMed:15567415,
FT ECO:0007744|PDB:1Q0Q"
FT BINDING 231
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000269|PubMed:15567415,
FT ECO:0007744|PDB:1Q0Q"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:12621040,
FT ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP"
FT MUTAGEN 14
FT /note="G->D: Loss of solubility and activity."
FT /evidence="ECO:0000269|PubMed:10787409"
FT MUTAGEN 153
FT /note="H->Q: Increase in KM for substrate. Reduces activity
FT 35-fold."
FT /evidence="ECO:0000269|PubMed:10787409"
FT MUTAGEN 209
FT /note="H->Q: Increase in KM for substrate. Reduces activity
FT 5000-fold."
FT /evidence="ECO:0000269|PubMed:10787409"
FT MUTAGEN 231
FT /note="E->K: No effect on KM for substrate. Reduces
FT activity by over 99.9%."
FT /evidence="ECO:0000269|PubMed:10787409"
FT MUTAGEN 257
FT /note="H->Q: Strong increase in KM for substrate. Loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:10787409"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1JVS"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 329..347
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:1Q0Q"
FT HELIX 375..395
FT /evidence="ECO:0007829|PDB:1Q0Q"
SQ SEQUENCE 398 AA; 43388 MW; 8B532683A4FF1207 CRC64;
MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS PRYAVMDDEA
SAKLLKTMLQ QQGSRTEVLS GQQAACDMAA LEDVDQVMAA IVGAAGLLPT LAAIRAGKTI
LLANKESLVT CGRLFMDAVK QSKAQLLPVD SEHNAIFQSL PQPIQHNLGY ADLEQNGVVS
ILLTGSGGPF RETPLRDLAT MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN
ASASQMEVLI HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV NSGVKPLDFC
KLSALTFAAP DYDRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ IRFTDIAALN
LSVLEKMDMR EPQCVDDVLS VDANAREVAR KEVMRLAS
