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
//