ID Z4WZB8_9PORP Unreviewed; 334 AA.
AC Z4WZB8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN Name=acoB {ECO:0000313|EMBL:EWC92769.1};
GN ORFNames=HMPREF0636_0795 {ECO:0000313|EMBL:EWC92769.1};
OS Porphyromonas catoniae ATCC 51270.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=887901 {ECO:0000313|EMBL:EWC92769.1, ECO:0000313|Proteomes:UP000023482};
RN [1] {ECO:0000313|EMBL:EWC92769.1, ECO:0000313|Proteomes:UP000023482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51270 {ECO:0000313|EMBL:EWC92769.1,
RC ECO:0000313|Proteomes:UP000023482};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-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}.
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:EWC92769.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JDFF01000011; EWC92769.1; -; Genomic_DNA.
DR RefSeq; WP_044168493.1; NZ_JDFF01000011.1.
DR AlphaFoldDB; Z4WZB8; -.
DR PATRIC; fig|887901.3.peg.698; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000023482; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:EWC92769.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000023482}.
FT DOMAIN 10..185
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 334 AA; 36510 MW; 73B76BB261DF743E CRC64;
MIEGQETKVM SVRDAIIEAM SEEMRRDENV FLIGEDVGVY GGDFGTSVGM LEEFGSERVR
DTPISENAIS GCAVGAALTG MRPIVDVTFM DFIVYMMDNI VNQAAKTRYM YGGKGSVPVV
FRCAAGSGLG SAAQHSQSLE AWFCNIPGLK VVAPGTPADV KGILKAAIRD NNPVIFLEYK
AQYNMKGEVP TSPDFVLPIG KADIKRVGKD VTVVTYGRML ERVLKAADKA LEKGIEVEVV
DLMTLMPLDK EAIINSVKKT GRVLLVNDAH KTGGFLGEIA ATITESDAFD YLDSRILRLA
AEDIPTPYNH SLEVAMLPDV NRILKYIERL YDKR
//
