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Database: UniProt
Entry: D1YZB7_METPS
LinkDB: D1YZB7_METPS
Original site: D1YZB7_METPS 
ID   D1YZB7_METPS            Unreviewed;       362 AA.
AC   D1YZB7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:BAI61789.1};
GN   Name=pdhA {ECO:0000313|EMBL:BAI61789.1};
GN   OrderedLocusNames=MCP_1717 {ECO:0000313|EMBL:BAI61789.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI61789.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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DR   EMBL; AP011532; BAI61789.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1YZB7; -.
DR   STRING; 304371.MCP_1717; -.
DR   KEGG; mpd:MCP_1717; -.
DR   PATRIC; fig|304371.9.peg.1753; -.
DR   eggNOG; arCOG01054; Archaea.
DR   InParanoid; D1YZB7; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:BAI61789.1}.
FT   DOMAIN          41..330
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   362 AA;  40570 MW;  D222CE9DE500C320 CRC64;
     MIDDKYLYRL EKGETFHILD QDGSANELDP KLPPDVLLKI YRMMVQARAF DEKALKLQRA
     GRMGTYPPLS GQEAVQIGSA FALDKSDWMV PSYREAGAMM VKGVPMKLQY MLWMGNDWGN
     RIPDGVNCLP VSIPVGSQTL HATGMAWAAN VRKEKNAFLC YFGDGATSRG DFHESLNFAG
     VFQVPAVFLC SNNGFAISTP VVLQTHAETI AQKAIAYGIR GYRLDGMDVL ASYVLAKDAL
     DRAKKGEGPT LIEALCYRFG PHTTADNPDL YREKEEVERI KKEKDPIARF RNYLVKRKLW
     DDQKEKALIE EIDRLVDAAA KEAEKAPVPT FEDLVRNVFA ETPPYLEDEL NYFKKVSGGG
     KP
//
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