ID A0A2I0MZV7_9CLOT Unreviewed; 889 AA.
AC A0A2I0MZV7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=ABB02_01525 {ECO:0000313|EMBL:PKK39293.1};
OS Clostridiaceae bacterium JG1575.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX NCBI_TaxID=1658742 {ECO:0000313|EMBL:PKK39293.1, ECO:0000313|Proteomes:UP000237298};
RN [1] {ECO:0000313|EMBL:PKK39293.1, ECO:0000313|Proteomes:UP000237298}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG1575 {ECO:0000313|EMBL:PKK39293.1,
RC ECO:0000313|Proteomes:UP000237298};
RA Nelson M.C., Graf J.;
RT "Draft genome of Clostridiaceae bacterium JG1575.";
RL Submitted (OCT-2015) 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: 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:PKK39293.1}.
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DR EMBL; LQGW01000052; PKK39293.1; -; Genomic_DNA.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000237298; Unassembled WGS sequence.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PS00551; MOLYBDOPTERIN_PROK_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000237298};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Selenium {ECO:0000313|EMBL:PKK39293.1};
KW Selenocysteine {ECO:0000313|EMBL:PKK39293.1}.
FT DOMAIN 1..75
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 75..114
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 135..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 179..207
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 214..270
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 347
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:PKK39293.1"
SQ SEQUENCE 889 AA; 98011 MW; A3AC37D7EF036B9A CRC64;
MKLTINGQPV EAEAKETILS ICQRSGIPIP TLCHDERLRP SGSCRLCLVE VGGRLDTACT
VPVREGMVVA TNTQRVRNAR RNVLDLLFSN HPNDCLTCSA SGRCRLQDYC YEYDVPMGSY
RQGARRHAPK DTSNKFYDFD PDKCILCGKC VRVCQELQCS DAIGWKDRGF GVKVAAAGGE
ALIDSPCVSC GNCVAVCPTG ALTEKHQKAR IWALEKTRTT CGFCGVGCQL DLLTHEDQVV
GVRPAFGTVP NDGLLCVKGR FAYHFINHNH RLKKPLIRRE GQLVEASWEE ALTLITEKIT
TIRKESGPDA IAGFSSARSS NEDNYMFQKM LRAGIGTNNV DHCARLUHSS TVAGLATTLG
SGAMTNAIGD TEFNDALFLI GTNTTENHPV IATLMKRAQR NGAKILVADP RRIEMAQRAD
RYLQIKPGSN IALINAMCHV IVRDGLTDQA FIKAQTEDFE ELAEFLKDYP PERMASVVGV
RAEEIEAAAH LYAEADCAGI YYAMGITQHS TGTHGVMALS NLALLTGNIG KAHAGINPLR
GQNNVQGACD MGCLPADFPG YQKVLKPEIR EFFEKAWERP LSGKVGLTLS EVLHAITEDQ
VRMLWVFGEN PAVSDPDTNH VLHALDHCEF LVVSDLFLTE TAEYADVVLP AASFAEKDGT
FTNTERRIQR IRRAVSPRGE SRPDWQVFLN ICQRLGMPKE YPDAKSVFEE IAQVTPSYRG
VSYERIESVG LQWPCPKKDH PGTSFLHGTR IARGRGLFVP VDYAPPMEVP DAAYPYVLTT
GRVLYQYHTM SMTGKTPALN ELTGDAYVEV SCETASRYNL KNGDRLRLRS RRGETTAAVR
ITDILEDDVL FMPFHFAQGA NMLTNTALDA IAKIPELKVC TVSIEKEVS
//
