ID   A0A075R9J6_BRELA        Unreviewed;       327 AA.
AC   A0A075R9J6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=BRLA_c019040 {ECO:0000313|EMBL:AIG26225.1};
OS   Brevibacillus laterosporus LMG 15441.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG26225.1, ECO:0000313|Proteomes:UP000005850};
RN   [1] {ECO:0000313|EMBL:AIG26225.1, ECO:0000313|Proteomes:UP000005850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG26225.1,
RC   ECO:0000313|Proteomes:UP000005850};
RX   PubMed=21914864; DOI=10.1128/JB.05696-11;
RA   Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT   "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT   invertebrates.";
RL   J. Bacteriol. 193:5535-5536(2011).
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; CP007806; AIG26225.1; -; Genomic_DNA.
DR   RefSeq; WP_003338541.1; NZ_CP007806.1.
DR   AlphaFoldDB; A0A075R9J6; -.
DR   STRING; 1042163.BRLA_c019040; -.
DR   KEGG; blr:BRLA_c019040; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_9; -.
DR   Proteomes; UP000005850; 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:AIG26225.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005850}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   327 AA;  35385 MW;  AEB2A8E73379E900 CRC64;
     MREITYLEAV REAMTQEMRV NPDVFLMGED IGVYGGAFGV SRGMIEEFGP ERIRNTPISE
     AAIAGAAVGA AMTGMRPIME LQFSDFITIA MDQLVNQAAK NRYMFGGKGK VPMVVRTPSG
     SGTGAAAQHT QSLEAWMAHI PGLKVVQPST AYDVKGLLKA AIDDHNPVIF YEHKLLYKTL
     GHVPEESYSI PLGVADVKRE GTDVTIVATA IMIHKALEAA TELEKEGISV EVIDPRTLVP
     LDTDTIIRSV KKTGKLIVVH EAVKFGGFGG EIVSMIAESE AFDYVDAPIR RLGGKSIPMP
     YNPVLEKAAI PQVPDIIQAV KDTVAHR
//