ID A0A0A2LMB1_9FLAO Unreviewed; 325 AA.
AC A0A0A2LMB1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=Q763_10535 {ECO:0000313|EMBL:KGO80446.1};
OS Flavobacterium beibuense F44-8.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1406840 {ECO:0000313|EMBL:KGO80446.1, ECO:0000313|Proteomes:UP000030129};
RN [1] {ECO:0000313|EMBL:KGO80446.1, ECO:0000313|Proteomes:UP000030129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F44-8 {ECO:0000313|EMBL:KGO80446.1,
RC ECO:0000313|Proteomes:UP000030129};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO80446.1}.
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DR EMBL; JRLV01000010; KGO80446.1; -; Genomic_DNA.
DR RefSeq; WP_035133929.1; NZ_JRLV01000010.1.
DR AlphaFoldDB; A0A0A2LMB1; -.
DR STRING; 1406840.Q763_10535; -.
DR eggNOG; COG0022; Bacteria.
DR Proteomes; UP000030129; Unassembled WGS sequence.
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 Pyruvate {ECO:0000313|EMBL:KGO80446.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030129}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 36040 MW; ACDBA0593009BD85 CRC64;
MRTIQFREAV CEAMSEEMRR DESVYLMGEE VAEYNGAYKA SKGMLDEFGP KRVIDTPIAE
LGFAGIAVGS AMNGNRPIVE FMTFNFSLVG IDQIINNAAK MRQMSAGQFS MPIVFRGPTA
SAGQLAATHS QAFENWFANT PGLKVVVPSN PYDAKGLLKS AIRDNDPVIF MESEQMYGDK
AEVPEGEYTI PLGVADIKRE GKDVTIVSFG KIIKEAFIAA DELEKEGISC EIIDLRTVRP
MDYDAILNSV KKTNRLVVLE EAWPFASVAS EITYMVQERA FDYLDAPVQR ITTADTPAPY
SPVLLKEWLP NSEDVVKAVK KVMYK
//
