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Database: UniProt
Entry: K0NDW5_DESTT
LinkDB: K0NDW5_DESTT
Original site: K0NDW5_DESTT 
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
//
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