ID A0A1I1KAM2_9RHOB Unreviewed; 965 AA.
AC A0A1I1KAM2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN05421762_1330 {ECO:0000313|EMBL:SFC55728.1};
OS Pseudooceanicola nitratireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=517719 {ECO:0000313|EMBL:SFC55728.1, ECO:0000313|Proteomes:UP000231644};
RN [1] {ECO:0000313|EMBL:SFC55728.1, ECO:0000313|Proteomes:UP000231644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29619 {ECO:0000313|EMBL:SFC55728.1,
RC ECO:0000313|Proteomes:UP000231644};
RA de Groot N.N.;
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=[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}.
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DR EMBL; FOLX01000001; SFC55728.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1KAM2; -.
DR STRING; 517719.SAMN05421762_1330; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000231644; 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; 2.
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:UP000231644}.
FT DOMAIN 22..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..139
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 177..208
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 221..250
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 257..313
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 965 AA; 105916 MW; A29C09F770F5B170 CRC64;
MKDFVIPPKD WDMGTPLPKS DATVTLKVDG FDVTVPEGTS VMRAAMQAGI RIPKLCATDS
VEAFGSCRLC LVEIEGRRGT PASCTTPVSQ GMSVRTQSDR LHKLRKGVME LYISDHPLDC
LTCSANGDCE LQDMAGMVGL RDVRYTATDQ PLATHHEART QGRDENFRYI PKDDSNPYFT
YDPAKCIVCS RCVRACEEVQ GTFALTIEGR GFDSRVSFGG ASDSVLSSDC VSCGACVQAC
PTATLQEKSV AEMGTPDRSV LTTCAYCGVG CSFKAELNGD KLVRMTPYKH GKANRGHSCV
KGRFAYGYAE HPDRILNPMI RDKVSDPWRE VSWDEAMQFT AARLTNIRET HGRKALGVIT
SSRCTNEETY LVQKLTRAVF MNNNTDTCAR VCHSPTGYGL GQTFGTSAGT QDFDSVEDTD
VVIVIGANPT DGHPVFASRL RKRLRQGATL IVIDPRRIDL LASPHMGASH HLPLRPGTNV
AVVSAIAHVI MTEGLADEDF IRTRCDWDDY AQYAEFIRDP RHAPETTELL TGVPAQALRE
AARAFATGGN GAIYYGLGVT EHSQGSTTVM GIANLAMLTG NIGRKGVGVN PLRGQNNVQG
SCDMGSFPHE LPGYRHVKNP EVRAIFESAW GVQIDPEPGL RIPNMLDAAV EGTFKALYVQ
GEDILQSDPD TKHVAAGLAA MDCVIVHDLF LNETANYAHV FLPGSSFLEK EGTFTNAERR
INRVREVMKP RNGYADWEIT QMLANAMGAG WHYTHPAQIM EEIAATTPSF ARVTYDLLEE
MGSVQWPCND ATPEGTPLMH VDAFVRGKGR FIVTEYVPTD EKTGPRFPLL LTTGRILSQY
NVGAQTRRTD NNVWHDQDLL EIHPHDAENR GIREGDWIRL ASRSGETTLR ATITDRVSPG
VVYTTFHHPD TQANVVTTDF SDWATNCPEY KVTAVQISPS NGPSDWQEDY AAQAEQARRI
LPAAE
//
