ID G5KGZ6_9STRE Unreviewed; 332 AA.
AC G5KGZ6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=acoB {ECO:0000313|EMBL:EHJ57091.1};
GN ORFNames=STRUR_1390 {ECO:0000313|EMBL:EHJ57091.1};
OS Streptococcus urinalis 2285-97.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ57091.1, ECO:0000313|Proteomes:UP000005388};
RN [1] {ECO:0000313|EMBL:EHJ57091.1, ECO:0000313|Proteomes:UP000005388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2285-97 {ECO:0000313|EMBL:EHJ57091.1};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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}.
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:EHJ57091.1}.
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DR EMBL; AEUZ02000001; EHJ57091.1; -; Genomic_DNA.
DR RefSeq; WP_006739821.1; NZ_AEUZ02000001.1.
DR AlphaFoldDB; G5KGZ6; -.
DR STRING; 764291.STRUR_1390; -.
DR eggNOG; COG0022; Bacteria.
DR Proteomes; UP000005388; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:EHJ57091.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005388}.
FT DOMAIN 7..182
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 332 AA; 36058 MW; 8F779B16C70F62EA CRC64;
MTETKLMALR EAVNLAMTEE MRKDDKIYLM GEDVGIYGGD FGTSVGMFEE FGAKRVRDTP
ISEAAISGAA IGSAITGLRP IVDVTFMDFL TIMMDAIVNN GAKNNYMFGG GLKTPVTFRV
ASGSGIGSAA QHSQSLEAWM THIPGIKVVA PGNANDAKGL LKSAIQDNNI VVFMEPKALY
GKKEEVNQDP DFYIPLGKGE IKREGSDLTI VSYGRMLERV LQAADEVAEE GIKVEVVDPR
TLVPLDKELI IDSIKKTGKV MLVNDAYKTG GYTAEIASMI TESEAFDYLD HPIVRLASED
VPVPYARVLE QAILPDVEKI KTAIRKMANK GN
//
