FDHB_WOLSU
ID FDHB_WOLSU Reviewed; 200 AA.
AC P27273;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Formate dehydrogenase iron-sulfur subunit;
GN Name=fdhB1; OrderedLocusNames=WS0028;
GN and
GN Name=fdhB2; OrderedLocusNames=WS0735;
GN and
GN Name=fdhB3; OrderedLocusNames=WS1147;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RX PubMed=1781728; DOI=10.1007/bf00290984;
RA Bokranz M., Gutmann M., Koertner C., Kojro E., Fahrenholz F.,
RA Lauterbach F., Kroeger A.;
RT "Cloning and nucleotide sequence of the structural genes encoding the
RT formate dehydrogenase of Wolinella succinogenes.";
RL Arch. Microbiol. 156:119-128(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- FUNCTION: This chain is an electron transfer unit containing 18
CC cysteine residues, 16 of which occur in four clusters.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Formate dehydrogenase is a membrane-bound complex, formed of
CC at least three different subunits.
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DR EMBL; X54057; CAA37990.1; -; Genomic_DNA.
DR EMBL; BX571657; CAE09201.1; -; Genomic_DNA.
DR EMBL; BX571659; CAE09854.1; -; Genomic_DNA.
DR EMBL; BX571660; CAE10234.1; -; Genomic_DNA.
DR PIR; S18214; S18214.
DR RefSeq; WP_011138001.1; NC_005090.1.
DR AlphaFoldDB; P27273; -.
DR SMR; P27273; -.
DR STRING; 273121.WS0028; -.
DR EnsemblBacteria; CAE09201; CAE09201; WS0028.
DR EnsemblBacteria; CAE09854; CAE09854; WS0735.
DR EnsemblBacteria; CAE10234; CAE10234; WS1147.
DR KEGG; wsu:WS0028; -.
DR KEGG; wsu:WS0735; -.
DR KEGG; wsu:WS1147; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_2_1_7; -.
DR OMA; MARMKFV; -.
DR OrthoDB; 1762646at2; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR000813; 7Fe_ferredoxin.
DR Pfam; PF13247; Fer4_11; 1.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Repeat; Transport.
FT CHAIN 1..200
FT /note="Formate dehydrogenase iron-sulfur subunit"
FT /id="PRO_0000159253"
FT DOMAIN 7..37
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 50..81
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 82..111
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 200 AA; 21761 MW; 7C54F3A583C5D0BE CRC64;
MESQARVKFY CDEARCIDCH GCDVACKEAH HLPVGVNRRR VVTLNEGLVG KEKSLSIACM
HCSDAPCAQV CPVDCFYVRA DGIVLHDKEK CIGCGYCLYA CPFGAPQFPK SGIFGSRGPM
DKCTFCAGGP EETHSEKEYK LYGQNRIAEG KVPVCAAMCS TKALLAGDSD SISLIIRERV
LKRGSGTASV PYTWSQAYKD
