ID A0A2T4Z0Y2_9BACL Unreviewed; 327 AA.
AC A0A2T4Z0Y2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN ORFNames=C8J48_3663 {ECO:0000313|EMBL:PTM53339.1};
OS Desmospora activa DSM 45169.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Desmospora.
OX NCBI_TaxID=1121389 {ECO:0000313|EMBL:PTM53339.1, ECO:0000313|Proteomes:UP000241639};
RN [1] {ECO:0000313|EMBL:PTM53339.1, ECO:0000313|Proteomes:UP000241639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45169 {ECO:0000313|EMBL:PTM53339.1,
RC ECO:0000313|Proteomes:UP000241639};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:PTM53339.1}.
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DR EMBL; PZZP01000004; PTM53339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4Z0Y2; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000241639; Unassembled WGS sequence.
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:PTM53339.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000241639}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 36138 MW; ACCCB108731C7BA9 CRC64;
MTKMNMSKAI NHAIRNEMHR DEKVLVYGED LGVAGGSWRV AENLQKEFGV TRVFDTPLAE
SAIAGMAVGL GYVGYRSVIE IEYSGFMFEA MDALAGQMAR VHYRSGGAFN APITVRVPFG
SGMGVVELHN DNLEGLLAQS HGLKVVMPSS PYDAKGLMIS AIRDNNPVIF FEHLSLYFNT
EEDVPEEEYM IEIDKASIKK EGHDVTLITY GAMVEKVMNV SKTIADKGIK AEVIDLRSLS
PIDYDTLITS IQKTKRAIII QEAQRSAGVA NIISSKLNEE LFTELKSPIS VIASPDTLHP
FVEVEDVWVS NENMIVDKIS SLFENQK
//
