ID B9DUL6_STRU0 Unreviewed; 333 AA.
AC B9DUL6;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN Name=pdhB {ECO:0000313|EMBL:CAR42430.1};
GN OrderedLocusNames=SUB1102 {ECO:0000313|EMBL:CAR42430.1};
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495 {ECO:0000313|EMBL:CAR42430.1, ECO:0000313|Proteomes:UP000000449};
RN [1] {ECO:0000313|Proteomes:UP000000449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J {ECO:0000313|Proteomes:UP000000449};
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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DR EMBL; AM946015; CAR42430.1; -; Genomic_DNA.
DR RefSeq; WP_012658589.1; NC_012004.1.
DR AlphaFoldDB; B9DUL6; -.
DR STRING; 218495.SUB1102; -.
DR KEGG; sub:SUB1102; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_9; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000000449; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
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;
KW Oxidoreductase {ECO:0000313|EMBL:CAR42430.1};
KW Pyruvate {ECO:0000313|EMBL:CAR42430.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000449}.
FT DOMAIN 7..182
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 333 AA; 36043 MW; 5EABCD2426094189 CRC64;
MSETKLMALR EAVNLAMTEE MRKDENIYLM GEDVGIYGGD FGTSVGMIEE FGPKRVKDTP
ISEAAISGAA IGSAITGLRP IVDVTFMDFL TIMMDAIVNN GAKNNYMFGG GLKTPVTFRV
ASGSGIGSAA QHSQSLEAWL THIPGIKVVA PGNANDAKGL LKSAIQDNNI VLFMEPKALY
GKKEEVNQDP DFYIPLGKGE IKREGTDLTI ISYGRMLERV LQAAEEVAEE GINVEVLDPR
TLVPLDKELI IESVKKTGKV MLVNDAYKTG GYIGEIATMI TESEAFDYLD HPIVRLASED
VPVPYARVLE QAILPDVEKI KAAIVKMAKN GNA
//
