ID A0A1B8TQR5_9FLAO Unreviewed; 327 AA.
AC A0A1B8TQR5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=LPB3_14325 {ECO:0000313|EMBL:OBY61959.1};
OS Polaribacter vadi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1774273 {ECO:0000313|EMBL:OBY61959.1, ECO:0000313|Proteomes:UP000092584};
RN [1] {ECO:0000313|Proteomes:UP000092584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0003 {ECO:0000313|Proteomes:UP000092584};
RA Shin S.-K., Yi H., Kim E.;
RL Submitted (FEB-2016) 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:OBY61959.1}.
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DR EMBL; LSFM01000025; OBY61959.1; -; Genomic_DNA.
DR RefSeq; WP_026775343.1; NZ_LSFM01000025.1.
DR AlphaFoldDB; A0A1B8TQR5; -.
DR STRING; 1774273.LPB03_14985; -.
DR KEGG; pob:LPB03_14985; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000092584; 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:OBY61959.1}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 36402 MW; 752A7B9F4BEAABCD CRC64;
MKTVQFREAI CEAMSEEMRR DESIYLMGEE VAEYNGAYKA SKGMLDEFGE KRVIDTPIAE
LGFAGIAIGS AMNGNRPIVE YMTFNFSLVG IDQIINNAAK IRQMSGGQFN CPIVFRGPTA
SAGQLGATHS QAFENWFANT PGLKVIVPSN PYDAKGLLKA AIRDDDPVIF MESEQMYGDK
MEIPEGEYII PIGVADIKRE GTDVTVVSFG KIIKEAYKAA EELEKEGISI EIIDLRTVRP
MDHDAILKSV KKTNRLVILE EAWPFGNVST EITYRIQEEA FDYLDAPIKR INTADTPAPY
SPVLFEKWIP NASDVVKAVK EVMYIKS
//
