ID B2A3S3_NATTJ Unreviewed; 893 AA.
AC B2A3S3;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN OrderedLocusNames=Nther_0100 {ECO:0000313|EMBL:ACB83699.1};
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB83699.1, ECO:0000313|Proteomes:UP000001683};
RN [1] {ECO:0000313|EMBL:ACB83699.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB83699.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RX PubMed=21642468; DOI=10.1128/JB.05157-11;
RA Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA Kyrpides N., Wiegel J.;
RT "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT Natranaerobius thermophilus JW/NM-WN-LF.";
RL J. Bacteriol. 193:4023-4024(2011).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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; CP001034; ACB83699.1; -; Genomic_DNA.
DR STRING; 457570.Nther_0100; -.
DR KEGG; nth:Nther_0100; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_9; -.
DR InParanoid; B2A3S3; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000001683; 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 InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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 Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 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; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000001683};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Selenium {ECO:0000313|EMBL:ACB83699.1};
KW Selenocysteine {ECO:0000313|EMBL:ACB83699.1}.
FT DOMAIN 2..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..119
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 139..172
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 220..276
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 353
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ACB83699.1"
SQ SEQUENCE 893 AA; 98461 MW; 992E626BBC59AFB9 CRC64;
MSLVTVTIDG QSIQVPKTST VLDACEKLGK EIPTLCHQKD LTTVGACRLC VVEVEGAGNF
PTACTLPVKD GMVINTNTDE VRHARKMVLE LLWANHPNDC LTCESNGNCK FQDYCYEYGV
TESRFRGEVI EHEIDETSRF VERDLDKCIL CGKCIRVCHE IQGSEAIDFM DRGFETKVAT
FYDKGLSDSP CVDCGNCINV CPVGALIPKP LKGKGRDYDF EKVKTTCPYC GVGCTFNLNV
KDGEVVGVSP DEEAEVNDGY LCVKGRFGTG FIHNDDRLTQ PLVRKNGELV ETDWEEALNT
VAENFKKLKE KHGGDAFGFL ASAKCTNEDN YLFQKFARAV VGTNNIDHCA RLUHAPTVAG
LATQFGSGAM TNSIGEIEDT STIFAIGTNT TEAHPIIAQK VFKAQNKGAK LIVADPRKIE
IAEKADIWLR PLPGTNVALL NGIMKVILEK DLVDKEFIRN NTEGFEEVKK QLEQVSLDEI
EQITQVPKDK IEQAAIMYGE SDKASTLYTM GITQHTTGTD AVSSIANLAL MTGNVGREST
GVNPLRGQNN VQGACDLGGL PNVLTGYQKV ADPETVSKFS QEWGQELNDQ PGMAVTEMLK
ATGEDLKAMY IMGENPMVTD ANLGHVEEAL DSLDFLVVQD IFLTETAEKA DVVLPASSFA
EKDGTFTNTE RRVQRVRKAI ESVGDSKPDW QIIADLSQQM GYEMNYSNPQ EIMDEIRKLT
PSYSGISYDR IEDQGIQWPC PSEDHPGTKY LHKEGNFAIG KGQFKAVDYR EPAETADDEY
PFVLTTGRML YHYHATMTRK VRELNEEVPE GDIEINTQDA EKLGIENGDQ VKVSSRRGEV
VTVAEVTDRV APGVVYMDFH YKEAAANRLT NDALDPAAKT PELKVSAVKV EKS
//
