ID E8PR89_THESS Unreviewed; 679 AA.
AC E8PR89;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Formate dehydrogenase, subunit alpha {ECO:0000313|EMBL:ADW21918.1};
GN OrderedLocusNames=TSC_c12980 {ECO:0000313|EMBL:ADW21918.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21918.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW21918.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
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; CP001962; ADW21918.1; -; Genomic_DNA.
DR RefSeq; WP_015717191.1; NC_014974.1.
DR AlphaFoldDB; E8PR89; -.
DR STRING; 743525.TSC_c12980; -.
DR KEGG; tsc:TSC_c12980; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_0; -.
DR Proteomes; UP000008087; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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}.
FT DOMAIN 1..53
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 679 AA; 75729 MW; 55AA92767D800910 CRC64;
MRTTCPYCGV GCQVEPEIQG GRILRVLAPD IPPNHGALCV KGRFGLDFAF SGKRLLYPMV
REDRRQAFRR VSWDEALDYT ASKLLAVLKR RGPEAIAVFP SAKTTNEEVY LTQKLARALL
STNHVDHCSR LCHSSSTVAL SRSLGGASMT NPIEDIWKTD LFLVVGSNTT ETHPVIGAMI
KKRVRQGAKL IVVDPRYTGM AEAATLWLRV RPGTDLFLLN AMARYILEEG LWDQGYVAER
TEGFAEWQAS LEPYTLEEAE RITGVEKERI ALAARLYATT KRAGAYWAMG VTQHTKGTAT
AQALVNLALL TGKVGKEGAG LNPLRGQNNV QGAGDMGALP DVLPGYLKVS DQAARKRFEA
LWGVELNPEP GLRMTEVFER IPEVEAIYLI GEDPVTSEPY QDHLKAKLEA LPFLVVQDIL
ENETTSFAHV VLPAASFLEK EGTFTNTDRR VQRIRKLLDP PGEARPDWWI VQELGKRLAQ
ALGRPWALYP GPEAIWEEVR RAIPEMMGGI TYRRLESEGV RWPCPHEDHP GEAVLFQKRF
NTPSGKARFF PVHFTPPAET PSEEYPFTLS TGRVLFHWHG GTLSRNSQLK EAYPELKVEV
NPKDAQKLGI GDGEIIQVVS RRGRIPARAW VTDRTPEGVV YAPFHFAEAP ANRLTLDALD
PFSRIPEYKV AAVRLEKLD
//
