FDHB_MEGG1
ID FDHB_MEGG1 Reviewed; 215 AA.
AC Q8GC87; P83237;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Formate dehydrogenase subunit beta;
DE Short=FDH subunit beta;
DE AltName: Full=Formate dehydrogenase small subunit;
GN Name=fdhB {ECO:0000312|EMBL:CAD20557.1};
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156, PROTEIN SEQUENCE OF 157-215,
RP SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FDHA.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX PubMed=12220497; DOI=10.1016/s0969-2126(02)00826-2;
RA Raaijmakers H., Macieira S.I.M.G., Dias J.M., Teixeira S., Bursakov S.,
RA Huber R., Moura J.J.G., Moura I., Romao M.J.;
RT "Gene sequence and the 1.8 A crystal structure of the tungsten-containing
RT formate dehydrogenase from Desulfovibrio gigas.";
RL Structure 10:1261-1272(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 157-215, METAL-BINDING, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RA Raaijmakers H., Macieira S.I.M.G., Dias J.M., Teixeira S., Bursakov S.,
RA Huber R., Moura J.J.G., Moura I., Romao M.J.;
RL Submitted (JAN-2002) to UniProtKB.
RN [3] {ECO:0000305}
RP FUNCTION.
RA Riederer-Henderson M.A., Peck H.D. Jr.;
RT "Properties of formate dehydrogenase from Desulfivibrio gigas.";
RL Can. J. Microbiol. 32:430-435(1986).
RN [4] {ECO:0000305}
RP SUBUNIT, AND FUNCTION.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX PubMed=10587462; DOI=10.1021/bi990069n;
RA Almendra M.J., Brondino C.D., Gavel O., Pereira A.S., Tavares P.,
RA Bursakov S., Duarte R., Caldeira J., Moura J.J.G., Moura I.;
RT "Purification and characterization of a tungsten-containing formate
RT dehydrogenase from Desulfovibrio gigas.";
RL Biochemistry 38:16366-16372(1999).
RN [5] {ECO:0000305}
RP METAL-BINDING, AND SUBUNIT.
RX PubMed=11372198; DOI=10.1007/s007750100215;
RA Raaijmakers H., Teixeira S., Dias J.M., Almendra M.J., Brondino C.D.,
RA Moura I., Moura J.J.G., Romao M.J.;
RT "Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: metal
RT identification and preliminary structural data by multi-wavelength
RT crystallography.";
RL J. Biol. Inorg. Chem. 6:398-404(2001).
CC -!- FUNCTION: Beta chain of the formate dehydrogenase (FDH) catalyzes the
CC reversible two-electron oxidation of formate to carbon dioxide. FDH
CC loses activity in the presence of air, but this activity can be
CC restored. This chain is an electron transfer unit.
CC {ECO:0000269|PubMed:10587462, ECO:0000269|Ref.3}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:11372198};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000269|PubMed:11372198};
CC -!- SUBUNIT: Heterodimer of alpha (FdhA) and beta (FdhB) subunits.
CC {ECO:0000269|PubMed:10587462, ECO:0000269|PubMed:11372198,
CC ECO:0000269|PubMed:12220497, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|Ref.2}.
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DR EMBL; AJ427412; CAD20557.1; -; Genomic_DNA.
DR PDB; 1H0H; X-ray; 1.80 A; B/L=2-215.
DR PDBsum; 1H0H; -.
DR AlphaFoldDB; Q8GC87; -.
DR SMR; Q8GC87; -.
DR STRING; 1121448.DGI_1364; -.
DR EvolutionaryTrace; Q8GC87; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR Pfam; PF13247; Fer4_11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Periplasm; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..215
FT /note="Formate dehydrogenase subunit beta"
FT /id="PRO_0000159221"
FT DOMAIN 3..32
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 129..168
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372198"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372198"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1H0H"
SQ SEQUENCE 215 AA; 23983 MW; 01A18C18901FEA2F CRC64;
MSKGFFVDTT RCTACRGCQV ACKQWHGNPA TPTENTGFHQ NPPDFNFHTY KLVRMHEQEI
DGRIDWLFFP DQCRHCIAPP CKATADMEDE SAIIHDDATG CVLFTPKTKD LEDYESVISA
CPYDVPRKVA ESNQMAKCDM CIDRITNGLR PACVTSCPTG AMNFGDLSEM EAMASARLAE
IKAAYSDAKL CDPDDVRVIF LTAHNPKLYH EYAVA
