ID D5XBZ2_THEPJ Unreviewed; 685 AA.
AC D5XBZ2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ADG81540.1};
GN OrderedLocusNames=TherJR_0670 {ECO:0000313|EMBL:ADG81540.1};
OS Thermincola potens (strain JR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC Thermincola.
OX NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG81540.1, ECO:0000313|Proteomes:UP000002377};
RN [1] {ECO:0000313|EMBL:ADG81540.1, ECO:0000313|Proteomes:UP000002377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR {ECO:0000313|EMBL:ADG81540.1,
RC ECO:0000313|Proteomes:UP000002377};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT "Complete sequence of Thermincola sp. JR.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP002028; ADG81540.1; -; Genomic_DNA.
DR STRING; 635013.TherJR_0670; -.
DR KEGG; tjr:TherJR_0670; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000002377; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
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; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; 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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 4: Predicted;
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:UP000002377};
KW Selenium {ECO:0000313|EMBL:ADG81540.1};
KW Selenocysteine {ECO:0000313|EMBL:ADG81540.1}.
FT DOMAIN 8..65
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 142
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ADG81540.1"
SQ SEQUENCE 685 AA; 75069 MW; 3117B5BA0453F82B CRC64;
MGRGGFPLKE VLTTCPYCGC GCGFYLTVNE KEEITGVVPS AEHPVSRGRL CVKGWNVFEF
INSPDRLLSP LVREGASLRE TGWDEALNKT AGKLKEIIKK YGPDAAGFFS SAKCTNEENY
LFMKFARAVV GTNNIDHCAR LUHSSTVAGL AASFGSGAMT NSIDEISQAD VILVTGSNTT
EQHPQVGAEI LKAVEEGAKL IVIDPRKIPL ADYATLYLQP KVGTNVAWLN GLAHVIIEEN
LCDRTFVDER TDGFAELQQV VKKYSPIYVE QLTGIPAGDL VKAARLYAGA DKAMIFYCMG
LTQFTSGVDN VRACANLAML TGNIGRPGTG VNPLRGQNNV QGACDMGALP NVLTGYQKVD
DEDARSKFEQ AWQVKLPAEP GLTLTEMIRA AEEGKIKCLY IMGENPLVSD PDINHVRKAF
EKLELLVVQD IFLTETAALA DIVLPGACFA EKEGTFTNTE RRVQRVRQAL APKGKAMEDW
RIILALACKM GYLMGYETPE EIMEEIAVLT PAYRGITYQR LEDEKGLQWP CPDMQHPGTP
YLHKDRFSCG RGKFHAVDYR PPAETPNDDY PYILTTGRTA YQFHTGTMTG RTSVIQREVP
DGYVEINKED AQKIGIRDGW PVEVSSARGK VVCRASVSDT VPAGTVFMPF HFAETAANLL
TNSAVDPIAK IPEYKVCAVK IKGVD
//
