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Database: UniProt
Entry: Q67J74_SYMTH
LinkDB: Q67J74_SYMTH
Original site: Q67J74_SYMTH 
ID   Q67J74_SYMTH            Unreviewed;       531 AA.
AC   Q67J74;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:BAD42276.1};
GN   OrderedLocusNames=STH3295 {ECO:0000313|EMBL:BAD42276.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD42276.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD42276.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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DR   EMBL; AP006840; BAD42276.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q67J74; -.
DR   SMR; Q67J74; -.
DR   STRING; 292459.STH3295; -.
DR   KEGG; sth:STH3295; -.
DR   eggNOG; COG3383; Bacteria.
DR   HOGENOM; CLU_000422_13_4_9; -.
DR   Proteomes; UP000000417; Chromosome.
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   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 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; IPR006478; Formate_DH_asu.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
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; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000417}.
FT   DOMAIN          6..332
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          417..523
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   531 AA;  58709 MW;  4700FEBD6B49C9E9 CRC64;
     MTNTINELQD MGPGDAIFAI GTNTTECHPI IGIRMLEAHR RGARLIVADP RETELAKHAD
     VYMRHNPGSD VALLNAMMYV IVTEGLADEA FIRSRTENFE ACRETVLKYA PEKVEGITGV
     PAEKVRQAAR LFATAENAAT YYTMGITQHT SGVDNVLSIA NLALMTGNLG KPKAGVNPLR
     GQNNVQGACD MGALPNVYPA YQPVTDPKNR EKFEKAWGRP LSDRMGMAIS DVLRGIEEGK
     VRFLYVMGEN PMRSDPDVNH VRHCLEHVDF LVVQDIFLTE SAALADVVLP GATWAEKDGT
     FTNTERRVQR VRKAMEPQGN ARPDWMILRD IMRAMDYPAD YNSPKDIFNE LRTLAPSYAG
     VTYERLEKLG GLHWPCPNEE HPGTPILHVG KFSRGLGKFS AIEWRPPAEL PDEEYPLVLT
     TGRRTAHYHT GTMTRNCWGL DGVAPEEWVE INPADAASLG VAHGDYVRVT TRRGSVVVRA
     EVTARVPKGV TFITFHYTEA AGNLLTNSAL DPVSKTPEYK VCAVRVEKVS A
//
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