ID F9YSZ2_CAPCC Unreviewed; 325 AA.
AC F9YSZ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN OrderedLocusNames=Ccan_06140 {ECO:0000313|EMBL:AEK22734.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK22734.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK22734.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(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; CP002113; AEK22734.1; -; Genomic_DNA.
DR RefSeq; WP_013996726.1; NC_015846.1.
DR AlphaFoldDB; F9YSZ2; -.
DR STRING; 860228.Ccan_06140; -.
DR KEGG; ccm:Ccan_06140; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_10; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000008895; 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:AEK22734.1};
KW Pyruvate {ECO:0000313|EMBL:AEK22734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 36047 MW; 7FEAE69FB50A7E52 CRC64;
MRTIQFREAI CEAMSEEMRR DESIYLMGEE VAEYNGAYKA SKGMLDEFGA KRVIDTPISE
LGFAGISVGA AMNGNRPIVE FMTFNFSLVG IDQIINNAAK MRQMSGGQFN IPIVFRGPTA
SAGQLAATHS QAFESWYANC PGLKVVVPSN PYDAKGLLKS AIRDNDPVIF MESEQMYGDK
GEVPEGEYTL PLGVADVKRE GKDVTIVSFG KIIKEAYAAA DQLAKEGIEC EIIDLRTVRP
MDHEAIFKSV RKTNRLVILE EAWPFGSVAS EITYQVQENV FDYLDAPIQR ITTADTPAPY
SPELLKEWLP NANDVIKAVK KVMYK
//
