ID   FRDA_SHEON              Reviewed;         596 AA.
AC   P83223;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Fumarate reductase flavoprotein subunit;
DE            EC=1.3.5.1;
DE   AltName: Full=Flavocytochrome c;
DE            Short=FL cyt;
DE   Flags: Precursor;
GN   OrderedLocusNames=SO_0970;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=MR-1;
RX   PubMed=11425747; DOI=10.1128/aem.67.7.3236-3244.2001;
RA   Tsapin A.I., Vandenberghe I., Nealson K.H., Scott J.H., Meyer T.E.,
RA   Cusanovich M.A., Harada E., Kaizu T., Akutsu H., Leys D., Van Beeumen J.J.;
RT   "Identification of a small tetraheme cytochrome c and a flavocytochrome c
RT   as two of the principal soluble cytochromes c in Shewanella oneidensis
RT   strain MR1.";
RL   Appl. Environ. Microbiol. 67:3236-3244(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
RN   [3] {ECO:0007744|PDB:1D4C, ECO:0007744|PDB:1D4D, ECO:0007744|PDB:1D4E}
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH FAD; HEMES C;
RP   FUMARATE AND SUCCINATE, AND COFACTOR.
RC   STRAIN=MR-1;
RX   PubMed=10581551; DOI=10.1038/70051;
RA   Leys D., Tsapin A.S., Nealson K.H., Meyer T.E., Cusanovich M.A.,
RA   Van Beeumen J.J.;
RT   "Structure and mechanism of the flavocytochrome c fumarate reductase of
RT   Shewanella putrefaciens MR-1.";
RL   Nat. Struct. Biol. 6:1113-1117(1999).
CC   -!- FUNCTION: Catalyzes fumarate reduction using artificial electron donors
CC       such as methyl viologen. The physiological reductant is unknown, but
CC       evidence indicates that flavocytochrome c participates in electron
CC       transfer from formate to fumarate and possibly also to trimethylamine
CC       oxide (TMAO). This enzyme is essentially unidirectional (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:10581551};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10581551};
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000269|PubMed:10581551};
CC       Note=Binds 4 heme c groups covalently per monomer.
CC       {ECO:0000269|PubMed:10581551};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10581551}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- INDUCTION: By anaerobiosis and fumarate. {ECO:0000269|PubMed:11425747}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the FAD-dependent
CC       oxidoreductase 2 family. FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; AE014299; AAN54044.1; -; Genomic_DNA.
DR   RefSeq; NP_716599.1; NC_004347.2.
DR   RefSeq; WP_011071245.1; NZ_CP053946.1.
DR   PDB; 1D4C; X-ray; 2.90 A; A/B/C/D=25-596.
DR   PDB; 1D4D; X-ray; 2.50 A; A=25-596.
DR   PDB; 1D4E; X-ray; 2.80 A; A=25-596.
DR   PDBsum; 1D4C; -.
DR   PDBsum; 1D4D; -.
DR   PDBsum; 1D4E; -.
DR   AlphaFoldDB; P83223; -.
DR   SMR; P83223; -.
DR   STRING; 211586.SO_0970; -.
DR   DrugBank; DB00518; Albendazole.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   DrugBank; DB01677; Fumaric acid.
DR   PaxDb; 211586-SO_0970; -.
DR   KEGG; son:SO_0970; -.
DR   PATRIC; fig|211586.12.peg.930; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_011398_4_5_6; -.
DR   OrthoDB; 9148689at2; -.
DR   PhylomeDB; P83223; -.
DR   BioCyc; SONE211586:G1GMP-903-MONOMER; -.
DR   EvolutionaryTrace; P83223; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08168; Cytochrom_C3; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010960; Flavocytochrome_c.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR012286; Tetrahaem_cytochrome.
DR   NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF14537; Cytochrom_c3_2; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF48695; Multiheme cytochromes; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; FAD; Flavoprotein; Heme; Iron;
KW   Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW   Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000305"
FT   CHAIN           26..596
FT                   /note="Fumarate reductase flavoprotein subunit"
FT                   /id="PRO_0000010345"
FT   REGION          142..596
FT                   /note="Flavoprotein-like"
FT   ACT_SITE        426
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0C278"
FT   BINDING         34
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         40
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         43
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         44
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         63
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         66
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         67
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         85
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         88
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         95
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         98
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         99
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         101
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         102
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         109
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         112
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         113
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         118
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         161
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         180
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         188
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         189
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         193
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         194
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         194
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4E"
FT   BINDING         194
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         195
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         225
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         368
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         385
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         389
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         401
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4E"
FT   BINDING         401
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         402
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4E"
FT   BINDING         402
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         528
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4E"
FT   BINDING         528
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         529
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         559
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         569
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4E"
FT   BINDING         569
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         572
FT                   /ligand="fumarate"
FT                   /ligand_id="ChEBI:CHEBI:29806"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4E"
FT   BINDING         572
FT                   /ligand="succinate"
FT                   /ligand_id="ChEBI:CHEBI:30031"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4D"
FT   BINDING         574
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   BINDING         575
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:10581551,
FT                   ECO:0007744|PDB:1D4C"
FT   CONFLICT        71
FT                   /note="K -> E (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="A -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            34..38
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           57..67
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           70..76
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:1D4C"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            132..135
FT                   /evidence="ECO:0007829|PDB:1D4C"
FT   HELIX           136..144
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          152..156
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          176..179
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           214..223
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            224..226
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           230..238
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           240..249
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          268..271
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            272..274
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           277..291
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          295..307
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:1D4C"
FT   STRAND          313..320
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            321..323
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          324..329
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           344..350
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           352..354
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           368..375
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          386..393
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            394..397
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           403..406
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          410..412
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           426..434
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           437..439
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          441..445
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           447..450
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           455..461
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          466..470
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           471..478
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           482..495
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            502..504
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          515..530
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          533..536
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   STRAND          541..556
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           558..560
FT                   /evidence="ECO:0007829|PDB:1D4C"
FT   STRAND          561..563
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   TURN            564..567
FT                   /evidence="ECO:0007829|PDB:1D4D"
FT   HELIX           573..591
FT                   /evidence="ECO:0007829|PDB:1D4D"
SQ   SEQUENCE   596 AA;  62448 MW;  74CB81FE89790463 CRC64;
     MFTRKIQKTA LAMLISGAMA GTAYAAPEVL ADFHGEMGGC DSCHVSDKGG VTNDNLTHEN
     GQCVSCHGDL KELAAAAPKD KVSPHKSHLI GEIACTSCHK GHEKSVAYCD ACHSFGFDMP
     FGGKWERKFV PVDADKAAQD KAIAAGVKET TDVVIIGSGG AGLAAAVSAR DAGAKVILLE
     KEPIPGGNTK LAAGGMNAAE TKPQAKLGIE DKKQIMIDDT MKGGRNINDP ELVKVLANNS
     SDSIDWLTSM GADMTDVGRM GGASVNRSHR PTGGAGVGAH VAQVLWDNAV KRGTDIRLNS
     RVVRILEDAS GKVTGVLVKG EYTGYYVIKA DAVVIAAGGF AKNNERVSKY DPKLKGFKAT
     NHPGATGDGL DVALQAGAAT RDLEYIQAHP TYSPAGGVMI TEAVRGNGAI VVNREGNRFM
     NEITTRDKAS AAILQQKGES AYLVFDDSIR KSLKAIEGYV HLNIVKEGKT IEELAKQIDV
     PAAELAKTVT AYNGFVKSGK DAQFERPDLP RELVVAPFYA LEIAPAVHHT MGGLVIDTKA
     EVKSEKTGKP ITGLYAAGEV TGGVHGANRL GGNAISDIVT YGRIAGASAA KFAKDN
//