ID A0A261W981_9BORD Unreviewed; 352 AA.
AC A0A261W981;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=CAL24_01780 {ECO:0000313|EMBL:OZI82627.1};
OS Bordetella genomosp. 2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1983456 {ECO:0000313|EMBL:OZI82627.1, ECO:0000313|Proteomes:UP000215633};
RN [1] {ECO:0000313|EMBL:OZI82627.1, ECO:0000313|Proteomes:UP000215633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU8256 {ECO:0000313|EMBL:OZI82627.1,
RC ECO:0000313|Proteomes:UP000215633};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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 -!- 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:OZI82627.1}.
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DR EMBL; NEVT01000002; OZI82627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261W981; -.
DR Proteomes; UP000215633; 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;
FT DOMAIN 10..185
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 352 AA; 37631 MW; D2C6D0881DECFAD8 CRC64;
MSNTGTARRL TMAQAISEAI GQEMERDERV FVMGEDVGKY GGIFSATTGL LDRFGKDRIM
DTPISETAFM GAALGAAAEG LRPISELMFV DFFGVCFDQI YNHIAKNTYM SGGAVKVPLV
ITTGIGGGYN DAAQHSQCLY SIFAHVPGLK VVVPSNAYDA KGLMIQAIRD DNPVVFLYHK
GIMGLTWMSY FEGSTTHVPA EAYALPFGEA AVVREGADLT IVTLSQMVQK SLVAAEQLQA
DGISAEILDL RTLVPLDKQA VLRSVARTGR LLVVDEDYLS FGLSGEIAAI VAENLDSVAL
KAPVRRLAVP DVPIPFSRPL EQFAIPQVDA IAQAARALVS GAAHATLTTT EN
//
