ID A0YAU7_9GAMM Unreviewed; 960 AA.
AC A0YAU7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=GP2143_04485 {ECO:0000313|EMBL:EAW31677.1};
OS marine gamma proteobacterium HTCC2143.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; BD1-7 clade.
OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW31677.1, ECO:0000313|Proteomes:UP000004931};
RN [1] {ECO:0000313|EMBL:EAW31677.1, ECO:0000313|Proteomes:UP000004931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW31677.1,
RC ECO:0000313|Proteomes:UP000004931};
RX PubMed=20601481; DOI=10.1128/JB.00683-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT isolated from the Oregon Coast.";
RL J. Bacteriol. 192:4530-4531(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAW31677.1}.
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DR EMBL; AAVT01000002; EAW31677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0YAU7; -.
DR STRING; 247633.GP2143_04485; -.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000004931; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000004931}.
FT DOMAIN 31..109
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 109..148
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 171..202
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 214..243
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 250..306
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 960 AA; 104795 MW; AE8A16962A2A0AAF CRC64;
MLQYYDPAKG LDVSKDYGTP AFNRQADRNT ELVNLTIDGR ELAVPAGTSI MRAAALADIS
IPKLCATDSL EAFGSCRMCL VEIAGRKGFP ASCTTSVEQG LVVRTQTDRV AKLRRNVMEL
YISDHPLDCL TCPANGNCEL QDVAGEVGLR DVRYGFDGKN HLSASKDTSN PYFTFDASKC
IVCSRCVRAC EEVQGTFALT IDGKGFDSVV AAGQAQSFME SDCVSCGACI QACPTSTLME
NTVIDQGQPQ RSVVTTCAYC GVGCAFKAEL KGDQVVRMVP HKGGEANRGH SCVKGRFAFG
YTTHQDRITT PMIRETIDDP WRKVSWDDAV NFAAARIKTI QQQYGRNSVG GITSSRCTNE
ETYLVQKLVR AAFGNNNVDT CARVCHSPTG YGLKTTLGES AGTQTFDSVE VADVVLVIGA
NPTDAHPVFA SRLKKRLRQG AQLIVADPRR IDLINSPHAN TPYHLKLLPG TNVAFINAIA
HVIVSEGLEA TEFIARRCDS EAFGRWKRFV KEQKNSPEAM ASITGVPAEQ LREAARVYAN
ANNGAIYYGL GVTEHSQGST MVMGIANLAM LTGNIGREGV GVNPLRGQNN VQGSCDMGSF
PHELPGYRHI SDDTVRHQFE QAWGVTLDHE PGFRIPNMLD AAVAGHYKGL YCQGEDIAQS
DPNTKHVEQA LRSLDCLIVQ DLFLNETANF AHVFLPGASF LEKDGTFTNA ERRISPVRKV
MSPLGGKADW EGTTALSNAL GYPMNYNHPS EIMDEIASLT PTFSGVSYQR LDQEGSLQWP
CNSAMPDGTP TMHVDEFVRG KGYFAITEYV ATDEKVNKRF PLLLTTGRIL SQYNVGAQTR
RTANVDWHER DLLEIHPHDA EDRGISDGDL VQVSSRAGKT VLTADVTERV QAGVTYTTFH
HPESGANVVT TDNSDWATNC PEYKVTAVEL KKVTAESSWQ RDHDAFSIKQ RGLVDTEVLP
//
