ID A0A1L8TL74_9ENTE Unreviewed; 325 AA.
AC A0A1L8TL74;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN ORFNames=RV04_GL002550 {ECO:0000313|EMBL:OJG45030.1};
OS Enterococcus hermanniensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=249189 {ECO:0000313|EMBL:OJG45030.1, ECO:0000313|Proteomes:UP000182077};
RN [1] {ECO:0000313|EMBL:OJG45030.1, ECO:0000313|Proteomes:UP000182077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17122 {ECO:0000313|EMBL:OJG45030.1,
RC ECO:0000313|Proteomes:UP000182077};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:OJG45030.1}.
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DR EMBL; JXKQ01000009; OJG45030.1; -; Genomic_DNA.
DR RefSeq; WP_071858391.1; NZ_JXKQ01000009.1.
DR AlphaFoldDB; A0A1L8TL74; -.
DR STRING; 249189.RV04_GL002550; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000182077; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 Pyruvate {ECO:0000313|EMBL:OJG45030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182077}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35327 MW; FEC6B7B2BB4ECF5B CRC64;
MAQKTMIQAI TDALALMLEK DKEVLIFGED VGKNGGVFRA TEGLQEKFGE DQVFDTPLAE
SGIAGLGFGL ALQGFRPVPE IQFFGFVFEA MDEIVGQMAR TRYRMGNTRN LPITIRAPFG
GGVHTPELHS DNLEGLMAQS PGLRVVIPSN PYDAKGLLIA SIRNNDPVVF LEHMKLYRSF
REEVPEGIYE VPLDKAAVTK EGSDISIITY GAMVREAIKA ADNLAKDNIN AEIIDLRTVA
PLDVETIIKS VEKTGRVVVV QEAQKQAGVS AQVISEISER AILSLEAPIG RVSAPDTIFP
FGQAEGIWLP NAADIEAKAR EIATF
//
