ID A0A0E3YSN7_9BACT Unreviewed; 324 AA.
AC A0A0E3YSN7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=IMCC26134_02795 {ECO:0000313|EMBL:AKC81969.1};
OS Verrucomicrobia bacterium IMCC26134.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1637999 {ECO:0000313|EMBL:AKC81969.1, ECO:0000313|Proteomes:UP000033046};
RN [1] {ECO:0000313|EMBL:AKC81969.1, ECO:0000313|Proteomes:UP000033046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26134 {ECO:0000313|EMBL:AKC81969.1,
RC ECO:0000313|Proteomes:UP000033046};
RA Choi A., Kang I., Cho J.-C.;
RT "Complete genome sequence of Verrucomicrobia strain IMCC26134.";
RL Submitted (APR-2015) 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; CP011265; AKC81969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3YSN7; -.
DR STRING; 1637999.IMCC26134_02795; -.
DR KEGG; vba:IMCC26134_02795; -.
DR PATRIC; fig|1637999.3.peg.597; -.
DR HOGENOM; CLU_012907_1_1_0; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000033046; Chromosome.
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:AKC81969.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033046}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 324 AA; 35228 MW; 15A64F3621B6A39A CRC64;
MPVLTYREAI RAALSEEIER DPNVVIMGEE VAQFNGAYKV TEGMLEKYGP KRIVDTPISE
AGFIGMGIGA SMLGIRPVME LMFWSFYSVA FDQIVNNAAN VRYMSGGQIA CPIVIRGPAN
GGTNVGATHS HTVENILAHH PGLKVVVPSN AADAKALMKT AIRDNDPVMF LENTILYGEK
GEVPEGDITL PFGRAAIART GKDLTIVTYG RCVLHSLAAA ETLRASKGFD IEIIDLRTIR
PLDVDTILRS VAKTHRLLIV EEQRPYCSIG SHIAAIVQEE AFDELDAPIL RVGTIDAPSI
YSPPVEKQQI PNVDRVIAGI LRLL
//
