ID A0A1I6CSL2_9RHOB Unreviewed; 927 AA.
AC A0A1I6CSL2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN04515673_101292 {ECO:0000313|EMBL:SFQ96122.1};
OS Poseidonocella sedimentorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871652 {ECO:0000313|EMBL:SFQ96122.1, ECO:0000313|Proteomes:UP000199302};
RN [1] {ECO:0000313|EMBL:SFQ96122.1, ECO:0000313|Proteomes:UP000199302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC {ECO:0000313|Proteomes:UP000199302};
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=[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}.
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DR EMBL; FOYI01000001; SFQ96122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6CSL2; -.
DR STRING; 871652.SAMN04515673_101292; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000199302; 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 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; 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:UP000199302}.
FT DOMAIN 8..88
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 145..175
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 188..217
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 230..285
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 927 AA; 101741 MW; B8BF1AF62578A2C8 CRC64;
MADGASVNMV TFSLNGEDVT VPEGITIWEA ANGRGLKIPH LCHKPAPGYR PDGNCRACMV
EVEGERTLVA SCIRPVSDGM VVKTETERAE KSRNLVMELL VADQPEKAHD RSSHFWDMAE
LNGVEESRFP KVEAETVPLL DASHVAMRVN LDACIHCNLC VRACREVQVN DVIGMAGRGH
TEQIVFDQND LMGDSTCVAC GECVQACPTG ALLPATVVDE NQEGDTKDFD REVKSVCPYC
GVGCQISFKV KDDKIKYVEG IDGPANQNRL CVKGRFGFDY IAHPHRLTKP LIRREDAPAK
GLNVDPGNLM THFREATWDE ALDAAANGLD RLRRDTGKRV AGFGSAKCSN EEAYLFQKLI
RQGFGHNNVD HCTRLCHASS VAALMENVGS GAVTATFNEI ENADVAIVIG CNPLENHPVA
ATYFKQFVKR GGKLIVMDPR SHGLKRFASH MLQFKPGGDV SMLNAIMNVI VEEGLYDQQY
IEAYTENWPA MKEHLKDYPP EKMEEICGVD AELLRDAART FATAKAGMIF WGMGVSQHIH
GTDNSRCLIS LALMTGQVGR PGTGLHPLRG QNNVQGASDA GMIPMFLPDY QSVMDDGVRS
AFTEVWESGD FSSEKGLTVV EIMDAIHAGD IRGMYILGEN PAMSDPDVDH ARDALAMLEH
LVVQDIFLTE TANYADVILP SSAFAEKTGT VTNTNRQVQM GRPVVAPPGE AKEDWWIEVE
LAKRLGLNWS YTHPREIFDE MKKNMASLDN ITWERLENAA VTYPSLSPED PGQAIVFGDG
FPRPEGRARF TPAAVIPPDE LPDPEYPFVL ITGRQLEHWH TGSMTRRATV LDAVEPEANC
SMHPHSLRDL GLAAGDIVRL TTRRGSIRLL VRADRAVAKG NVFLPFAYVE AAANILTNAA
LDPYGKIPEF KFAAVKVEKD QDAIAAE
//