FADH_ECOLI
ID FADH_ECOLI Reviewed; 672 AA.
AC P42593; Q2M9C5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing] {ECO:0000303|PubMed:10933894, ECO:0000303|PubMed:9346310};
DE Short=DCR {ECO:0000303|PubMed:12840019};
DE EC=1.3.1.34 {ECO:0000269|PubMed:18171025, ECO:0000269|PubMed:6363415, ECO:0000269|PubMed:9346310};
DE AltName: Full=2,4-dienoyl-coenzyme A reductase [NADPH] {ECO:0000305|PubMed:6363415};
GN Name=fadH {ECO:0000303|PubMed:9346310}; Synonyms=ygjL;
GN OrderedLocusNames=b3081, JW3052;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=9346310; DOI=10.1111/j.1432-1033.1997.00516.x;
RA He X.-Y., Yang S.-Y., Schulz H.;
RT "Cloning and expression of the fadH gene and characterization of the gene
RT product 2,4-dienoyl coenzyme A reductase from Escherichia coli.";
RL Eur. J. Biochem. 248:516-520(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, SUBUNIT, INDUCTION, AND PATHWAY.
RX PubMed=6363415; DOI=10.1016/s0021-9258(17)43476-4;
RA Dommes V., Kunau W.H.;
RT "2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli.
RT Comparison of properties.";
RL J. Biol. Chem. 259:1781-1788(1984).
RN [5]
RP FUNCTION, COFACTOR, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=10933894; DOI=10.1006/abbi.2000.1941;
RA Liang X., Thorpe C., Schulz H.;
RT "2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur
RT flavoprotein that functions in fatty acid beta-oxidation.";
RL Arch. Biochem. Biophys. 380:373-379(2000).
RN [6]
RP CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF
RP GLU-165; TYR-167; HIS-253 AND CYS-338.
RC STRAIN=K12;
RX PubMed=18171025; DOI=10.1021/bi701235t;
RA Tu X., Hubbard P.A., Kim J.J., Schulz H.;
RT "Two distinct proton donors at the active site of Escherichia coli 2,4-
RT dienoyl-CoA reductase are responsible for the formation of different
RT products.";
RL Biochemistry 47:1167-1175(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-672 IN COMPLEX WITH
RP 5-MERCAPTOETHANOL-2-DECENOYL-COENZYME A; FAD; FMN; IRON-SULFUR (4FE-4S) AND
RP NADP, COFACTOR, DOMAIN, REACTION MECHANISM, AND ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=12840019; DOI=10.1074/jbc.m304642200;
RA Hubbard P.A., Liang X., Schulz H., Kim J.J.;
RT "The crystal structure and reaction mechanism of Escherichia coli 2,4-
RT dienoyl-CoA reductase.";
RL J. Biol. Chem. 278:37553-37560(2003).
CC -!- FUNCTION: Functions as an auxiliary enzyme in the beta-oxidation of
CC unsaturated fatty acids with double bonds at even carbon positions.
CC Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the
CC acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA
CC (PubMed:9346310, PubMed:6363415). Acts on both isomers, 2-trans,4-
CC cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency
CC (PubMed:6363415). Is not active with NADH instead of NADPH
CC (PubMed:6363415). Does not show cis->trans isomerase activity
CC (PubMed:10933894). {ECO:0000269|PubMed:10933894,
CC ECO:0000269|PubMed:6363415, ECO:0000269|PubMed:9346310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4,5-saturated-(2E)-enoyl-CoA + NADP(+) = a (2E,4E)-dienoyl-
CC CoA + H(+) + NADPH; Xref=Rhea:RHEA:12136, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85100,
CC ChEBI:CHEBI:85101; EC=1.3.1.34;
CC Evidence={ECO:0000269|PubMed:18171025, ECO:0000269|PubMed:6363415,
CC ECO:0000269|PubMed:9346310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(2E)-
CC enoyl-CoA + NADP(+); Xref=Rhea:RHEA:45232, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85099,
CC ChEBI:CHEBI:85100; EC=1.3.1.34;
CC Evidence={ECO:0000269|PubMed:6363415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-CoA + NADP(+) = (2E,4E)-decadienoyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:53296, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61406, ChEBI:CHEBI:62244;
CC Evidence={ECO:0000269|PubMed:18171025, ECO:0000269|PubMed:6363415,
CC ECO:0000269|PubMed:9346310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-CoA + NADP(+) = (2E,4Z)-decadienoyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:53708, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:61406, ChEBI:CHEBI:137593;
CC Evidence={ECO:0000269|PubMed:6363415};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:10933894, ECO:0000269|PubMed:12840019};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10933894, ECO:0000269|PubMed:12840019,
CC ECO:0000269|PubMed:6363415};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10933894, ECO:0000269|PubMed:12840019};
CC -!- ACTIVITY REGULATION: Is non-competitively inhibited by NADH.
CC {ECO:0000269|PubMed:6363415}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for NADPH {ECO:0000269|PubMed:9346310};
CC KM=10.1 uM for NADPH {ECO:0000269|PubMed:6363415};
CC KM=2.3 uM for (2E,4E)-decadienoyl-CoA {ECO:0000269|PubMed:9346310};
CC KM=8.8 uM for (2E,4E)-decadienoyl-CoA {ECO:0000269|PubMed:6363415};
CC KM=4.1 uM for (2E,4Z)-decadienoyl-CoA {ECO:0000269|PubMed:6363415};
CC Note=kcat is 16 sec(-1) for the NADPH-reduction of (2E,4E)-
CC decadienoyl-CoA. {ECO:0000269|PubMed:9346310};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:10933894, ECO:0000305|PubMed:6363415}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6363415}.
CC -!- INTERACTION:
CC P42593; P11349: narH; NbExp=3; IntAct=EBI-561933, EBI-555067;
CC P42593; P19318: narY; NbExp=3; IntAct=EBI-561933, EBI-555059;
CC -!- INDUCTION: Induced when cells are grown on oleate as sole carbon
CC source. Repressed by glucose. {ECO:0000269|PubMed:6363415}.
CC -!- DOMAIN: Is composed of three domains: an N-terminal TIM barrel
CC (residues 1-368) which binds FMN, the 4Fe-4S cluster, and the
CC substrate; a flavodoxin-like fold (residues 369-467 and 626-671) which
CC binds FAD; and an NADP(H)-binding domain (residues 468-625).
CC {ECO:0000269|PubMed:12840019}.
CC -!- MISCELLANEOUS: The overall reaction mechanism can be divided into three
CC stages: initially, reduction of FAD by NADPH, then electron transfer
CC from FAD to FMN via the 4Fe-4S cluster, and finally reduction of
CC substrate. {ECO:0000305|PubMed:12840019}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U93405; AAB82738.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57882.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76116.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77131.1; -; Genomic_DNA.
DR PIR; F65096; F65096.
DR RefSeq; NP_417552.1; NC_000913.3.
DR RefSeq; WP_000121433.1; NZ_LN832404.1.
DR PDB; 1PS9; X-ray; 2.20 A; A=2-672.
DR PDBsum; 1PS9; -.
DR AlphaFoldDB; P42593; -.
DR SMR; P42593; -.
DR BioGRID; 4261984; 17.
DR BioGRID; 851910; 4.
DR DIP; DIP-9562N; -.
DR IntAct; P42593; 10.
DR STRING; 511145.b3081; -.
DR DrugBank; DB03698; 5-Mercaptoethanol-2-decenoyl-coenzyme A.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03247; Flavin mononucleotide.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR SwissLipids; SLP:000001817; -.
DR jPOST; P42593; -.
DR PaxDb; P42593; -.
DR PRIDE; P42593; -.
DR EnsemblBacteria; AAC76116; AAC76116; b3081.
DR EnsemblBacteria; BAE77131; BAE77131; BAE77131.
DR GeneID; 947594; -.
DR KEGG; ecj:JW3052; -.
DR KEGG; eco:b3081; -.
DR PATRIC; fig|511145.12.peg.3176; -.
DR EchoBASE; EB2582; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_1_6; -.
DR InParanoid; P42593; -.
DR OMA; QFLAAHT; -.
DR PhylomeDB; P42593; -.
DR BioCyc; EcoCyc:DIENOYLCOAREDUCT-MON; -.
DR BioCyc; MetaCyc:DIENOYLCOAREDUCT-MON; -.
DR BRENDA; 1.3.1.34; 2026.
DR UniPathway; UPA00659; -.
DR EvolutionaryTrace; P42593; -.
DR PRO; PR:P42593; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033543; P:fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway; IMP:EcoCyc.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; FMN;
KW Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9346310"
FT CHAIN 2..672
FT /note="2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-
FT producing]"
FT /id="PRO_0000194482"
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12840019,
FT ECO:0000305|PubMed:18171025"
FT BINDING 25..27
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 59
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 101
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 215
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 253..256
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 289
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 311..312
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 335
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 338
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 340
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 342
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 354
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 385
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 412
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 449
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 563..564
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 567
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 578
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 649
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 654..656
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT BINDING 656..658
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12840019,
FT ECO:0007744|PDB:1PS9"
FT SITE 253
FT /note="Important for catalytic activity, assists active
FT site Tyr in protonation of C4"
FT /evidence="ECO:0000305|PubMed:12840019,
FT ECO:0000305|PubMed:18171025"
FT MUTAGEN 165
FT /note="E->A: Exhibits 1.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:18171025"
FT MUTAGEN 165
FT /note="E->Q: Loss of enzyme activity; when associated with
FT Ala-167."
FT /evidence="ECO:0000269|PubMed:18171025"
FT MUTAGEN 167
FT /note="Y->F: Forms 3-enoyl-CoA as the product of the
FT reaction instead of 2-enoyl-CoA, at a rate which is 26% of
FT wild-type. 2-fold increase in substrate affinity. Loss of
FT enzyme activity; when associated with Gln-165."
FT /evidence="ECO:0000269|PubMed:18171025"
FT MUTAGEN 253
FT /note="H->A: 1000-fold reduction in enzyme activity. Forms
FT both 3-enoyl-CoA and 2-enoyl-CoA as products of the
FT reaction."
FT /evidence="ECO:0000269|PubMed:18171025"
FT MUTAGEN 253
FT /note="H->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:18171025"
FT MUTAGEN 338
FT /note="C->A: 1000-fold reduction in enzyme activity. Highly
FT affects iron-sulfur cluster binding."
FT /evidence="ECO:0000269|PubMed:18171025"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 53..64
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 134..153
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 188..206
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 270..276
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 399..409
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 425..439
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 484..488
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 525..531
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 568..571
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 596..601
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 634..638
FT /evidence="ECO:0007829|PDB:1PS9"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:1PS9"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:1PS9"
FT HELIX 658..671
FT /evidence="ECO:0007829|PDB:1PS9"
SQ SEQUENCE 672 AA; 72678 MW; B26C7CAAACE760C3 CRC64;
MSYPSLFAPL DLGFTTLKNR VLMGSMHTGL EEYPDGAERL AAFYAERARH GVALIVSGGI
APDLTGVGME GGAMLNDASQ IPHHRTITEA VHQEGGKIAL QILHTGRYSY QPHLVAPSAL
QAPINRFVPH ELSHEEILQL IDNFARCAQL AREAGYDGVE VMGSEGYLIN EFLTLRTNQR
SDQWGGDYRN RMRFAVEVVR AVRERVGNDF IIIYRLSMLD LVEDGGTFAE TVELAQAIEA
AGATIINTGI GWHEARIPTI ATPVPRGAFS WVTRKLKGHV SLPLVTTNRI NDPQVADDIL
SRGDADMVSM ARPFLADAEL LSKAQSGRAD EINTCIGCNQ ACLDQIFVGK VTSCLVNPRA
CHETKMPILP AVQKKNLAVV GAGPAGLAFA INAAARGHQV TLFDAHSEIG GQFNIAKQIP
GKEEFYETLR YYRRMIEVTG VTLKLNHTVT ADQLQAFDET ILASGIVPRT PPIDGIDHPK
VLSYLDVLRD KAPVGNKVAI IGCGGIGFDT AMYLSQPGES TSQNIAGFCN EWGIDSSLQQ
AGGLSPQGMQ IPRSPRQIVM LQRKASKPGQ GLGKTTGWIH RTTLLSRGVK MIPGVSYQKI
DDDGLHVVIN GETQVLAVDN VVICAGQEPN RALAQPLIDS GKTVHLIGGC DVAMELDARR
AIAQGTRLAL EI
