ID A0A1H0HB67_9GAMM Unreviewed; 942 AA.
AC A0A1H0HB67;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN04487957_10497 {ECO:0000313|EMBL:SDO16392.1};
OS Halomonas shengliensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=419597 {ECO:0000313|EMBL:SDO16392.1, ECO:0000313|Proteomes:UP000199075};
RN [1] {ECO:0000313|Proteomes:UP000199075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6444 {ECO:0000313|Proteomes:UP000199075};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; FNIV01000004; SDO16392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0HB67; -.
DR STRING; 419597.SAMN04487957_10497; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000199075; 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; cd02790; MopB_CT_Formate-Dh_H; 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; IPR041925; CT_Formate-Dh_H.
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 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 PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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}.
FT DOMAIN 4..84
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 164..194
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 207..236
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 249..304
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 942 AA; 100903 MW; C686E8A80DE557C6 CRC64;
MTQETFTLTL DGVEVDARPG ETLWQVARRA GETIPHLCFK DAPGYRADGN CRACMVEVEG
ERVLAASCIR EAAPGMVVKS ADSARAREAR EGVMELLLAD QPAREASPDR SSHLWSMADR
LAIDAGAVRE RLPARAEREA PTVHHVAERS AALPHAHGHD ASHSAMSVNL DACIECGLCV
RACREVQAND VIGLAHRGAA AKVVFDFDDP MGESTCVACG ECVQACPTGA LMPATLIDEA
GRGDSAAADR RVDSICPYCG VGCQLTYHVK DEQILFVEGR NGPSNQGRLC VKGRFGFDYP
GHPARLTRPL IRRPGVPKGL DPDFDPARPL THFREASWEE ALDLAARGLV ELKATQGPDA
LAGFGSAKCS NEEAWLFQKL VRVGFGSNHV DHCTRLCHAS SVAALMECLG SGAVTASFMQ
ALQAEVVILT GCNPAVNHPV AATYFKQAAR NGTKLIILDP RGQALDAYAW RSLRFSPGGD
VALFNAMLNV IIGEGLYDPA YIDAHTEGFA ALKAGVVDMT PEAMSPLCGV APEAIREVAR
AYAGAERAMI FWGMGISQHV HGTDNARCLI SLALACGHTG RPGTGLHPLR GQNNVQGASD
AGLIPMVLPD YQPVGDAQLR AAFEALWGTE LAPDPGLTVV EIMDAILAGQ IRGMYILGEN
PAMSDPDLNH ARAALAALEH LVVQDLFVTE TAQFADVILP AAAWSEKTGT VTNTNRQVQL
GRAALAPPGE AKPDWWIIQQ MARRFGLGWD YAHPREVFAE MKRGMHSLDH ITWERLEREG
SVTYPCPADD APGQDVVFAD AFPRAGGRAR FSPTRPLPPD EPVDAAYPVV LTTGRLLEHW
HTGAMTRRSR VLDEREPEAA AFLAPAELGR LGVAPGGAVR IATRRGAITL TARVDPGMPE
GMVFVPFAFV EAAANLLTNP ALDPDGKIPE FKYAACRLSP AS
//
