ID K0NDW5_DESTT Unreviewed; 923 AA.
AC K0NDW5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 08-NOV-2023, entry version 61.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN Name=fdhA {ECO:0000313|EMBL:CCK79101.1};
GN OrderedLocusNames=TOL2_C09330 {ECO:0000313|EMBL:CCK79101.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79101.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79101.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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; FO203503; CCK79101.1; -; Genomic_DNA.
DR STRING; 651182.TOL2_C09330; -.
DR KEGG; dto:TOL2_C09330; -.
DR HOGENOM; CLU_000422_4_0_7; -.
DR OMA; YIPTMCY; -.
DR OrthoDB; 9757870at2; -.
DR Proteomes; UP000007347; Chromosome.
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; 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:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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; 2.
DR SMART; SM00926; Molybdop_Fe4S4; 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; 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:UP000007347};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Selenium {ECO:0000313|EMBL:CCK79101.1};
KW Selenocysteine {ECO:0000313|EMBL:CCK79101.1}.
FT DOMAIN 1..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 162..196
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 207..236
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 245..301
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 378
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:CCK79101.1"
SQ SEQUENCE 923 AA; 102680 MW; 7448DC3C673897B2 CRC64;
MISGGIVLNG REYPFKKGQT ILDVARQNRI DIPTLCYFKG VVSKGSCNIC VVEVKGVKDL
VPACSTEIMG RMDIRTESPR VVAARKKTLK AILESGNHNC SIGASQGDSW TRFQLDVMQM
ENHHELCPKW GDCELQDLAY RYQVQWNRTS LSDCRFPRET VNPLIIRDFS RCILCGRCVA
ACNDIQVNQA IRMPKQTENQ RIIAGMDDVA LKDSDCVFCG ECVQACPVGA LVEKKIEHQW
RPWEIEKIRT TCPYCGVGCQ LWLHVKEDKI LKVTGVEDAA PNKGRLCVKG RFGFDFIYSQ
ERLTTPLIKK NGAFQQASWD EALDLVAEKF KTIIRESGPD ALAGVSCARS INEDSYQMQK
LFRAVFKTNN IDHCARTUHA PTVAGLATTF GSGAMTNSFS EFARAKMILV IGSNMTQAHP
VAATFVKNAV QNGAGLIVVD PRKHRLTDFA DIHLQLKVGS DIALLNGIMH VLIKEELYDK
EFSLNKCTGF EDLEKTVAQY SPDKAARISG VDEDTIIQTA RLLASVKPAM VCYTLGITEH
TCGKNNVMTV ANLQMLLGNM GMELGGVNPL RGQNNVQGAC DMGALPNVFH GYQNVADPNA
RQKFETAWQV TNLPEKPGLM IPQMMHGLTN GSVRAFYIFG ENLANTEPDM NKVAKELEAA
EFTVCQDLFL TETTRFADVV LPAAAWSENN GTFTNSERRV SRVRTAGRPP GLARPNWWIF
KQIAKRFGHD WSASSAREIW DKEISPLAPA LEGIKYHRIG RDGLQWPCPT LDHPGTPYLH
QDGNFTHGKG VFMPTQWTPP AEVPDEEYPF VLSTGRRLYH YHTRTQTGRC EGLNDLLGEE
TADISQADAD RMGIAPGERI RVRSRRGEVC VSANVTHEVP LGMVWMAFHF TEGNANWLTN
SALDPSTLTA EYKACAVQLE KIL
//