ID F4CZ09_PSEUX Unreviewed; 328 AA.
AC F4CZ09;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN OrderedLocusNames=Psed_2075 {ECO:0000313|EMBL:AEA24300.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA24300.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA24300.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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; CP002593; AEA24300.1; -; Genomic_DNA.
DR RefSeq; WP_013674231.1; NC_015312.1.
DR AlphaFoldDB; F4CZ09; -.
DR STRING; 675635.Psed_2075; -.
DR KEGG; pdx:Psed_2075; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:AEA24300.1};
KW Pyruvate {ECO:0000313|EMBL:AEA24300.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 4..178
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 328 AA; 34476 MW; 43498817C7A194B0 CRC64;
MARLKYWQAI NQALREEMAR DEAVCVLGED VGAPGGPFGA TKGLLDEFGA ARVRDTPISE
ATIVGAALGA SMTGLRPVVE VMFLDFMTVA MDQVVNQAAK VGYMSGGHYR APMVVRTICA
SGRNTGPQHA QNLEAWLAHV PGLTVVWGSN PADARGLLKS AIRDDGPVVV IESLAEWSRR
GEVADDPDAL VPIGVAAVRR PGTDVTVVTW GGAVHRVDAA AAALADEVDV EVIDLRTISP
WDRATVLESV RRTGRLVVVH DAVAAFGAGA EIAATVAEHC FGDLRAPVTR VAAPFAPSPF
PPQLEAAYLP QPGTIADAIR ASVLQGVR
//
