ID A0A0C2VP23_9BACL Unreviewed; 340 AA.
AC A0A0C2VP23;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=KP78_06430 {ECO:0000313|EMBL:KIL50642.1};
OS Jeotgalibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=889306 {ECO:0000313|EMBL:KIL50642.1, ECO:0000313|Proteomes:UP000031938};
RN [1] {ECO:0000313|EMBL:KIL50642.1, ECO:0000313|Proteomes:UP000031938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P9 {ECO:0000313|EMBL:KIL50642.1,
RC ECO:0000313|Proteomes:UP000031938};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Genome sequencing of Jeotgalibacillus soli.";
RL Submitted (JAN-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:KIL50642.1}.
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DR EMBL; JXRP01000008; KIL50642.1; -; Genomic_DNA.
DR RefSeq; WP_041086226.1; NZ_JXRP01000008.1.
DR AlphaFoldDB; A0A0C2VP23; -.
DR STRING; 889306.KP78_06430; -.
DR PATRIC; fig|889306.3.peg.641; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000031938; 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:KIL50642.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031938}.
FT DOMAIN 9..184
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 340 AA; 37388 MW; 06B1ABEC3BF38BFF CRC64;
METIEKRMLT GNKAMAEAIA LEMERDPTVF VLGEDVGKYG GIFGSTQGLF DQFGADRVMD
TPISETAFIG AAIGAAAEGM RPITELMFVD FFGVCMDQIY NHMAKIPYMS GGNVKLPMVL
MTAVGGGYND AAQHSQTLYA TFAHLPGMKV VAPSTPYDLK GMMISAIRDD NPVVFMFHKT
LQGLGWMDQL DASISHVPKE DYTVPLDKAN VVREGKDVTI VGLQMTMHYA LEAAEKLAEE
GIEAEVIDLR SIAPIDKETI IKSVKRTHRL IVVDEDYLSC GISAEVSAII AEEALYELEA
PVKRIAVPDV PLPYSRPLEQ FVLPNANKIY DEAMKLINEW
//
