ID   A0A3L9YDV2_9FLAO        Unreviewed;       325 AA.
AC   A0A3L9YDV2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=BXY75_2423 {ECO:0000313|EMBL:RMA57620.1};
OS   Ulvibacter antarcticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=442714 {ECO:0000313|EMBL:RMA57620.1, ECO:0000313|Proteomes:UP000271339};
RN   [1] {ECO:0000313|EMBL:RMA57620.1, ECO:0000313|Proteomes:UP000271339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23424 {ECO:0000313|EMBL:RMA57620.1,
RC   ECO:0000313|Proteomes:UP000271339};
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 (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:RMA57620.1}.
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DR   EMBL; REFC01000014; RMA57620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L9YDV2; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000271339; 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   Pyruvate {ECO:0000313|EMBL:RMA57620.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271339}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   325 AA;  35774 MW;  F6BEF5AE9C8D6401 CRC64;
     MKTLQFREAI CEAMSEEMRR DESIYLMGEE VAEYNGAYKA SKGMLDEFGA KRVIDTPIAE
     LGFSGIAIGS AMNGNRPIVE YMTFNFSLVG IDQIINNAAK IRQMSGGQFN CPIVFRGPTA
     SAGQLGATHS QAFESWFANC PGLKVVVPSN PADAKGLLKS AIRDNDPVIF MESEQMYGDK
     GEVPEGEYLI PLGVAEIKRK GNDVTIVSFG KIIKEAYKAA ETLAEEGIDC EIIDLRTVRP
     MDTNTILESV KKTNRLVILE EAWPFGNVAT EITYQVQSQI FDYLDAPIVK INTADTPTPY
     SPGLLAEWLP NSEDVVKAVK KVMYK
//