ID C3GN73_BACTU Unreviewed; 325 AA.
AC C3GN73;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=bthur0010_37100 {ECO:0000313|EMBL:EEM76430.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM76430.1};
RN [1] {ECO:0000313|EMBL:EEM76430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM76430.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
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:EEM76430.1}.
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DR EMBL; ACNH01000068; EEM76430.1; -; Genomic_DNA.
DR RefSeq; WP_000068166.1; NZ_CM000755.1.
DR AlphaFoldDB; C3GN73; -.
DR SMR; C3GN73; -.
DR GeneID; 83637679; -.
DR HOGENOM; CLU_012907_1_0_9; -.
DR Proteomes; UP000006660; Chromosome.
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:EEM76430.1}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35229 MW; 5B8175602690FB58 CRC64;
MAQMTMIQAI TDALRVEMKN DPNVLVFGED VGVNGGVFRA TEGLQAEFGE DRVMDTPLAE
SGIGGLAVGL ALEGFRPVPE IQFFGFVYEV MDSISGQLAR MRYRSGGRWT APVTVRSPFG
GGVHTPELHA DSLEGLVAQQ PGLKVVIPST PYDAKGLLIS AIRDNDPVIY LEHMKLYRSF
RQDVPEGEYT IDLGKADIKR EGTDVSVIAY GAMVHAALKA AEELEKEGIS LEVVDLRTVQ
PLDIETIIAS VEKTGRVVVV QEAQKQAGIA ANVVAEINDR AILNLEAPVV RVAAADTVFP
FSQAESVWLP NHKDIVEAVN KVMNF
//
