ID   G2J491_PSEUL            Unreviewed;       727 AA.
AC   G2J491;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:BAK76886.1};
GN   OrderedLocusNames=NH8B_2071 {ECO:0000313|EMBL:BAK76886.1};
OS   Pseudogulbenkiania sp. (strain NH8B).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK76886.1, ECO:0000313|Proteomes:UP000001274};
RN   [1] {ECO:0000313|Proteomes:UP000001274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX   PubMed=22038961; DOI=10.1128/JB.06127-11;
RA   Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT   "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT   Pseudogulbenkiania sp. strain NH8B.";
RL   J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK76886.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2J491; -.
DR   STRING; 748280.NH8B_2071; -.
DR   KEGG; pse:NH8B_2071; -.
DR   eggNOG; COG3383; Bacteria.
DR   HOGENOM; CLU_000422_4_0_4; -.
DR   Proteomes; UP000001274; Chromosome.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
DR   GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
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; 3.40.50.740; -; 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; 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   PIRSF; PIRSF000144; CbbBc; 2.
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; PS00932; MOLYBDOPTERIN_PROK_3; 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   Reference proteome {ECO:0000313|Proteomes:UP000001274}.
FT   DOMAIN          15..71
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   727 AA;  80006 MW;  5B778A4550DE09F8 CRC64;
     MPILPQHHIQ FGQPEHSKIT TCAYCGVGCG FKAEMKGNQV VRMTPWKDGK ANEGHACVKG
     RFAWGYATHP DRITKPMIRS KITDPWREVS WDEAIAYAAS EFKRLQAKYG KDSIGGITSS
     RCTNEETYLV QKLIRAGFGN NNVDTCARVC HSPTGYGLGQ TYGTSAGTQT FKSIEQTDVV
     LVIGANPTDA HPVFGSRMKK RLREGAKLIV IDPRQIDLIN SPHIQADYHL PLKPGTNVAM
     ITALAHVIVT EGLLADDFIA ERCEEKSFHD WKDFVAKPEN SPEATAEITG VPAELVRGAA
     RLYATGGNAA IYYGLGVTEH SQGSTMVIGI ANLAMATGNI GREGVGVNPL RGQNNVQGSC
     DMGSFPHELP GYRHISDDAT RHLFEDAWGV TLDPEPGLRI PNMFDAALSG SFMGLYCEGE
     DIVQSDPNTQ HVTAALSAME CIVVQDIFLN ETAKYAHVFL PGSSFLEKDG TFTNAERRIS
     RVRQVMKPLA KYADWEVTQL LANALGLKMD YTHPSQIMDE IARLTPSFAG VSYEKIDKHG
     SVQWPCNDDA PDGTPTMHID GFVRGKGKFF VTQYIATDEK VNRRFPLILT TGRILSQYNV
     GAQTRRTANS MWHPEDVLEI HPHDAEERGI KDGDSVAVTS RAGETVLHAK VSERMQPGVV
     YTTFHFPESG ANVITTDNSD WATNCPEYKV TAVQVLPVTQ PSEWQQSYQR FNQTQLELLE
     QAGEGKA
//