ID   Q877E4_METMI            Unreviewed;       674 AA.
AC   Q877E4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:AAO85928.1};
GN   Name=fdhA1 {ECO:0000313|EMBL:AAO85928.1};
OS   Methanococcus maripaludis (Methanococcus deltae).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=39152 {ECO:0000313|EMBL:AAO85928.1};
RN   [1] {ECO:0000313|EMBL:AAO85928.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LL/S2 {ECO:0000313|EMBL:AAO85928.1};
RX   PubMed=12670979; DOI=10.1128/JB.185.8.2548-2554.2003;
RA   Wood G.E., Haydock A.K., Leigh J.A.;
RT   "Function and regulation of the formate dehydrogenase genes of the
RT   methanogenic archaeon Methanococcus maripaludis.";
RL   J. Bacteriol. 185:2548-2554(2003).
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};
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DR   EMBL; AY236515; AAO85928.1; -; Genomic_DNA.
DR   BRENDA; 1.17.98.3; 3262.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
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; cd02790; MopB_CT_Formate-Dh_H; 1.
DR   CDD; cd02753; MopB_Formate-Dh-H; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; 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   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   4: Predicted;
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   Selenium {ECO:0000313|EMBL:AAO85928.1};
KW   Selenocysteine {ECO:0000313|EMBL:AAO85928.1}.
FT   DOMAIN          3..59
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   NON_STD         132
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000313|EMBL:AAO85928.1"
SQ   SEQUENCE   674 AA;  74225 MW;  9DAB8BE5FCEDA186 CRC64;
     MELDFIHTIC PYCGTGCGVD LVVKDGTLVG TNPFKRHPVN EGKTCIKGSY CHEFVHRDDR
     LKTPLIRKNG ELVEASWDEA LELISGKLQN YSPEEVGFFS SARCTNEDNY VFQKFARTVI
     KTNNVDHCAR LUHSATVVGL GQAFGSGAMT NSISDIEDAD CIFIIGSNTF EQHPLIARRV
     VRAKEKGTKI IVIDPRYTPT AKQADLYLQL LPGTNIAVLN AIMHVLVKEN LVDEEFIKNR
     TKGYEELKTT LETYTPEYAS KLSGVAPELI VEAAKMYGSA NAASILYCMG ITQFTTGVNN
     VKSCCNLAMI TGNIGKPGTG VNPLRGQNNV QGACDMGALP NVFPGYQAVP ANHEKYAEAW
     NTCVDPNVGL SIPDMLAKAG EQVKCIYVMG ENPMVSDPDI HHVEHALKSL DLLIVQDIFL
     TETAQVADVV LPGASWAEKD GTFSNTERRI QKINKAVDSP GEAIADWKIV KMLAEKMGQG
     ELFNFNTAEE VFQEIAKVTP QYAGVTYERL GVDGLHWPCK TCEDPGTPIL HCEKCLTPDG
     LGNIFAIDYA DPDEMADSEY PMTLTTGRII FHYHTGTMTR RSKHMADEIN EGFVEIHPED
     AEKMGIKNKQ KVKVSTRRGE VVVNAKITPN IKQGVVFMPF HFAETAANIL TNPAQDPNCK
     IPEYKVCAAK VEKI
//