ID   A0A1I5U882_9PSED        Unreviewed;       343 AA.
AC   A0A1I5U882;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=SAMN05216190_12426 {ECO:0000313|EMBL:SFP91470.1};
OS   Pseudomonas borbori.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=289003 {ECO:0000313|EMBL:SFP91470.1, ECO:0000313|Proteomes:UP000198784};
RN   [1] {ECO:0000313|Proteomes:UP000198784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17834 {ECO:0000313|Proteomes:UP000198784};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOWX01000024; SFP91470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5U882; -.
DR   STRING; 289003.SAMN05216190_12426; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000198784; 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:SFP91470.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          10..185
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   343 AA;  37112 MW;  60FC7C3D3A665449 CRC64;
     MTTAVKQRKL TVARAMAEAV AQEMRLDPRV FVMGEDIGPL GGVFGNTRGL HEEFGGARVR
     DTPISETAFI GAAVGAASDG MRPIVELMFV DFFGVCMDAI YNLMAKNTYF SGGKVRVPMV
     LMASTGAGYS DAGQHSQCLY ATFAHLPGMK VVVPSNAYDA KGLMTAAIRD DNPVIFLFHK
     ALQGMGWLGT EKGATVAVPE EPYCLEIGKA KTLREGSDVS IVSLGVGVHH ALRAAQQLEQ
     DGVSAEVIDL RSLVPLDRDH VIASVRKTGR LIVVDEDYHS FGVSGEIIAS VVEHDIGMLK
     ARPQRVAFPD IPIPFTPVME QWALPNAEKI VAAYQQMHEE QNR
//