ID A0A024HLR7_PSEKB Unreviewed; 323 AA.
AC A0A024HLR7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN Name=PDH2 {ECO:0000313|EMBL:CDF85554.1};
GN ORFNames=PKB_4229 {ECO:0000313|EMBL:CDF85554.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF85554.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF85554.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF85554.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF85554.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF85554.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-2014) 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; HG322950; CDF85554.1; -; Genomic_DNA.
DR RefSeq; WP_043254133.1; NZ_HG322950.1.
DR AlphaFoldDB; A0A024HLR7; -.
DR STRING; 1301098.PKB_4229; -.
DR KEGG; pkc:PKB_4229; -.
DR PATRIC; fig|1301098.3.peg.4236; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_6; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000025241; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:CDF85554.1};
KW Pyruvate {ECO:0000313|EMBL:CDF85554.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000025241};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 323 AA; 34745 MW; F4FD8DAC28603434 CRC64;
MSHTTYREAL REALREALLR DERVFLMGED VGRYGGSYAV SKGLLEEFGE ARIRDTPLSE
LTFVGAGIGA ALGGMRPIVE VMTVNFSLLA LDPLVNTAAT LRHMSGGQFS VPLVLRMATG
AGRQLAAQHS HSLEGWLAHI PGLKILAPAT LEDARGMLWP ALQDPDPVLI FEHAQLYNLE
GELDADAPVD IRSAKVRREG SDLTLIAYGG TLHKALAAAE QLAQEGISAE VIDLRVLRPL
DDATLLASLR KTRRVLVVDE AWRSGGLSAE ILARLTEQGF YELDAPPARL CSAEVPIPYA
KHLEDAALPQ VPGIVAAARG LLG
//
