ID   A0A0M9WTI6_9BACI        Unreviewed;       326 AA.
AC   A0A0M9WTI6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=AN161_19270 {ECO:0000313|EMBL:KOS61123.1};
OS   Lysinibacillus sp. FJAT-14222.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1932366 {ECO:0000313|EMBL:KOS61123.1, ECO:0000313|Proteomes:UP000037693};
RN   [1] {ECO:0000313|EMBL:KOS61123.1, ECO:0000313|Proteomes:UP000037693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17725 {ECO:0000313|EMBL:KOS61123.1,
RC   ECO:0000313|Proteomes:UP000037693};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) 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:KOS61123.1}.
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DR   EMBL; LIYL01000046; KOS61123.1; -; Genomic_DNA.
DR   RefSeq; WP_053595960.1; NZ_LIYL01000046.1.
DR   AlphaFoldDB; A0A0M9WTI6; -.
DR   STRING; 1932366.AN161_19270; -.
DR   PATRIC; fig|380630.3.peg.5986; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000037693; 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:KOS61123.1}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   326 AA;  35488 MW;  BBC5F12256740063 CRC64;
     MREISYSEAV KEAMTQVMRE DNDVFIMGED IGVYGGAFGV TSGMIDEFGP ERVRITPISE
     AAISGCAVGS AMTGMRPILE IQFSDFVVIA MDNIVNQAAK MRYMFGGKAK VPMVVRLPAG
     SGAGFAAQHS QSLEAWMTHI PGLKVVQPSN AYDAKGLLKA AIKDDNPVLF YEHKMLYNLK
     GDVPEESYEI PLGVADIKRE GKDITIIATG MMVNHAVEAA QQLEQEGIDV EVIDPRTLVP
     LDEKAILESV KKTGRVLVVY EAVKRGGFGT EIVSLIAESD AFDYLDAPIL RLGGVEAPIP
     YNPKLEKAAI PQVSDIYQKC LELMNK
//