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Database: UniProt
Entry: A0A0P7WVP5_9RHOB
LinkDB: A0A0P7WVP5_9RHOB
Original site: A0A0P7WVP5_9RHOB 
ID   A0A0P7WVP5_9RHOB        Unreviewed;       923 AA.
AC   A0A0P7WVP5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE            EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN   Name=fdoG-2 {ECO:0000313|EMBL:KPQ04742.1};
GN   ORFNames=HLUCCA12_16455 {ECO:0000313|EMBL:KPQ04742.1};
OS   Rhodobacteraceae bacterium HLUCCA12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ04742.1, ECO:0000313|Proteomes:UP000050476};
RN   [1] {ECO:0000313|EMBL:KPQ04742.1, ECO:0000313|Proteomes:UP000050476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ04742.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-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=[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:KPQ04742.1}.
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DR   EMBL; LJSV01000026; KPQ04742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7WVP5; -.
DR   STRING; 1666916.HLUCCA12_16455; -.
DR   PATRIC; fig|1666916.3.peg.1620; -.
DR   Proteomes; UP000050476; 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   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; 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; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 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; 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   Oxidoreductase {ECO:0000313|EMBL:KPQ04742.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..81
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          140..170
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          179..212
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          225..280
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   923 AA;  100227 MW;  137FC8DE940B8588 CRC64;
     MSVTFTLDGR DVTAEPGQTI WEVANGRGLV IPHLCHKPAA GYRPDGNCRA CMVEIEGERV
     LAASCIREPA EGMVVHTATE RARKSRALVM ELLLADQPER AAAHDRSSHL WAMAEAQGVH
     DNRFPTLEAG RIPVPDDSHV AMRVNLDACI QCGLCVRACR EVQVNDVIGM AGRGHDAWPV
     FDFDDPMGDS TCVACGECVQ ACPTGALMPA TVLDDAQQGD SAAHEHETRS ICPFCGVGCQ
     VSLKVRDGRI THVEGINGPA NEARLCVKGR FGFDYIHHPH RLTVPLIRRD DAPKGLDVDP
     ENPLTHFREA SWDEALDAAA GGLKRLAETH GGAAVAGFGS AKCSNEEAYL FQKLIRQGFG
     HNNVDHCTRL CHASSVAALM ENVGSGAVTA TFNEIANADC AIVIGANPVE NHPVAATYFK
     QFAKRGGKLI VMDPRGQALK RHATHMLQFK PGADVAMLNA IMHVIVTEGL ADRQYIQAMT
     ENWEAMTSHL ADFSPEAMEP VCGIPAETLR AVAHDFATSR AGMIFWGMGV SQHIHGTDNS
     RCLISLALMC GHVGRPGTGL HPLRGQNNVQ GASDAGLIPM FLPDYQNVSD DRIRERFVSL
     WDNTEFSGEK GLTVTEILDA VHDGQIKGMY ILGENPAMSD PDVTHAREAL AALEHLVVQD
     IFLTETANYA DVILPAAAFY EKTGTVTNTN RQVQLGRAAL PPPGQARADW AVTAELAKRL
     GLNWTYQHPR EVFAEMALTM KSLSNITWDR LEREGAVTYP SLAPDDPGQA IVFGDGFPRP
     SGRARFTPAR IIAPDELPDA DYPMVLTTGR QLEHWHTGSM TRRSRVLDAV EPEANCSLHP
     ATLRHLGVAP GGRVRLSTRR GTIELLARAD RSVSENMVFL PFAFVEAAAN ILTNPALDPY
     GKIPEFKFAA VRVEKARENA EAE
//
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