ID   A0A2S8RYY7_9RHOB        Unreviewed;       336 AA.
AC   A0A2S8RYY7;
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};
GN   ORFNames=LX70_03756 {ECO:0000313|EMBL:PQV53749.1};
OS   Defluviimonas denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Defluviimonas.
OX   NCBI_TaxID=404881 {ECO:0000313|EMBL:PQV53749.1, ECO:0000313|Proteomes:UP000238338};
RN   [1] {ECO:0000313|EMBL:PQV53749.1, ECO:0000313|Proteomes:UP000238338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18921 {ECO:0000313|EMBL:PQV53749.1,
RC   ECO:0000313|Proteomes:UP000238338};
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 (FEB-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:PQV53749.1}.
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DR   EMBL; PVEP01000012; PQV53749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8RYY7; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000238338; 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:PQV53749.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238338}.
FT   DOMAIN          12..187
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   336 AA;  35826 MW;  662398DE73FF7885 CRC64;
     MNAQTRTEMR ELSYAEAIRE AMDIALASDD RVILMGEDIG VYGGAFQVTG DLVEKYGTDR
     VMDTPISELG GAGVAVGAAL TGLKPIFEFQ FSDFAALAME QIVNQAAKVR YMLGGSVSVP
     LVMRFPAGSG TGAAAQHSQS IEAWLGHVPG LKVVQPSTPE DVKGMLLAAL EDPDPVMIFE
     HKILYKMKGH VPEGHYTTPI GKAAIRRAGK DLTIVATSLM VHKALAAAET LGPEGIDVEV
     IDLRTIRPMD RETVLASVRK TGRLICVYEG VKTLGVGAEI SAMVAESDAF DFLDAPIVRL
     GGAECPIPYN PELEKAVVPQ VPDILDAARN LAEGRI
//