ID   A0A3S0W662_9BACI        Unreviewed;       328 AA.
AC   A0A3S0W662;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 10.
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=ELQ35_11975 {ECO:0000313|EMBL:RUQ28627.1};
OS   Peribacillus cavernae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1674310 {ECO:0000313|EMBL:RUQ28627.1, ECO:0000313|Proteomes:UP000267430};
RN   [1] {ECO:0000313|EMBL:RUQ28627.1, ECO:0000313|Proteomes:UP000267430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L5 {ECO:0000313|EMBL:RUQ28627.1,
RC   ECO:0000313|Proteomes:UP000267430};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT   sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT   Center where the Viking Spacecraft were Assembled.";
RL   Submitted (DEC-2018) 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:RUQ28627.1}.
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DR   EMBL; RYZZ01000015; RUQ28627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0W662; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000267430; 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:UP000267430}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   328 AA;  35466 MW;  A5DE0669A9B0AE50 CRC64;
     MREITYAEAI NEVMCQEIEA NEDVFILGED IGIYGGAFGL TRGMIEKLGP EKVLNTPISE
     QAITGVAIGA ALMGMRPILE LQFSDFVTVA MDQIVNQAAK IRYMYGGKGK VPIVIRTPGG
     SGAGFAAQHS QSLEAWMAHI PGLKVVQPST AYDAKGLFRA ALEDDNPVIF YEHKLLYGMK
     DDVPEESYVI PLGKADIKRE GKDVTVVATS IMVHRALQAA EELEKEGISV EVIDPRTLVP
     LDIETIVESV KKTGRAVVVY EAVQRGGYGA EIASVINEGE AFDYLDAPVV RLGGKAVPIP
     YNPTLEKKAV PQVEDIINAI KSTVVTYA
//