ID A0A430A7R6_9ENTE Unreviewed; 325 AA.
AC A0A430A7R6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 8.
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=CBF31_05395 {ECO:0000313|EMBL:RSU03152.1};
OS Vagococcus fessus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=120370 {ECO:0000313|EMBL:RSU03152.1, ECO:0000313|Proteomes:UP000287101};
RN [1] {ECO:0000313|EMBL:RSU03152.1, ECO:0000313|Proteomes:UP000287101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 41755 {ECO:0000313|EMBL:RSU03152.1,
RC ECO:0000313|Proteomes:UP000287101};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:RSU03152.1}.
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DR EMBL; NGJY01000002; RSU03152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430A7R6; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000287101; 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 Reference proteome {ECO:0000313|Proteomes:UP000287101}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35206 MW; 346E1C807A8091E4 CRC64;
MAQKTMIQAI TDALAVELEK DPNVLIFGED VGNNGGVFRA TEGLQAKFGE DRVMDAPLAE
SGIGGMAFGL ALEGYRPVPE IQFFGFIFEV MDEVVAQMAR TRYRMGGTRH MPITIRAPFG
GGVHTPELHA DNLEGLIAQS PGIRVVIPSN PYDAKGLLIS AIRDNDPVVF LEHMKLYRSF
REEVPDGEYT VPLDKAAVTK EGKDVSIITY GAMVRESIKA AEKLEAAGIS VEIIDLRTVA
PLDIETIIAS VEKTGRVVVV QEAQKQAGVA AQVISEISER AVLSLEAPIG RVPAPDTIFP
FGQAENAWLP NAADIEAKVK EVYEF
//
