ID A0A3N0BMM2_9SPHI Unreviewed; 328 AA.
AC A0A3N0BMM2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=D7004_19240 {ECO:0000313|EMBL:RNL49553.1};
OS Pedobacter jejuensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1268550 {ECO:0000313|EMBL:RNL49553.1, ECO:0000313|Proteomes:UP000274046};
RN [1] {ECO:0000313|EMBL:RNL49553.1, ECO:0000313|Proteomes:UP000274046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNB23 {ECO:0000313|EMBL:RNL49553.1,
RC ECO:0000313|Proteomes:UP000274046};
RA Cho Y.-J., Cho A., Kim O.-S.;
RT "Genome sequencing of Pedobacter jejuensis TNB23.";
RL Submitted (OCT-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 -!- 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:RNL49553.1}.
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DR EMBL; RBEE01000045; RNL49553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0BMM2; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000274046; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
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:RNL49553.1};
KW Pyruvate {ECO:0000313|EMBL:RNL49553.1}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 328 AA; 36061 MW; BA2EF2552A9BE20D CRC64;
MREIQFREAL REAMSEEMRK DDRVFLLGEE VAEYNGAYKV SQGMLDEFGE KRIIDTPIAE
LGFAGIATGA ATAGLIPIVE FMTFNFSLVA IDQIINGAAK ILSMSGGQFS CPMVFRGPTG
NAGQLGAQHS QNFENWFANT PGLKVVVPST PYEAKGLLKQ AIIDPDPVIF MESEVMYGDK
GDVPAEEYYI EFGKANVTKQ GTDVTIVTFG KMLTRVVNPA VEELTKEGIN VEVIDLRTVR
PIDYDTIIES VKKTNRLVVV EEAWPLASLS GEIAFMVQKK AFDYLDAPVI RITCADVPLP
YSPTLIAASL PNAEKVIKAV KEVMYVKK
//
