ID   A0A0G1Y7S2_9BACT        Unreviewed;       332 AA.
AC   A0A0G1Y7S2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=UY89_C0021G0005 {ECO:0000313|EMBL:KKW39498.1};
OS   Parcubacteria group bacterium GW2011_GWA1_54_9.
OC   Bacteria.
OX   NCBI_TaxID=1618802 {ECO:0000313|EMBL:KKW39498.1, ECO:0000313|Proteomes:UP000033905};
RN   [1] {ECO:0000313|EMBL:KKW39498.1, ECO:0000313|Proteomes:UP000033905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKW39498.1}.
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DR   EMBL; LCRU01000021; KKW39498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1Y7S2; -.
DR   Proteomes; UP000033905; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR   PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          6..180
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   332 AA;  36913 MW;  95D401C5FFF38052 CRC64;
     MNNREISYKE AIREAFEEEL AENPRLIVIG EDIRESKSGI SLLTECENKF PGRIMNHLPL
     VEEMLGGIAL GMNLAGFKPA VQMDYSTFIT LMMSDIFEIG NWRYRMGEEA GPGITIRLSH
     EGYGEKGAEL GASLLALLLH IPNLAIATPS IPYYAKGLLK TALRAEFPTI FFEHKRLYDI
     RGRVPEGEYT VPFGTSAIFK PGNDVTIVSW SYLTHQALTA ARALQEEGVS AEVISLETLH
     PLRIEPLVAS VRKTGRLLIV EEDMERGGVG GEIAAEVIQR VPSLRIERLA AHNVGLPPTK
     RELFFLPTVE KIAAAARDLA KSGTRRWFRL RS
//