ID   A0A2A4S850_9CHLR        Unreviewed;       321 AA.
AC   A0A2A4S850;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=COB68_09965 {ECO:0000313|EMBL:PCI17304.1};
OS   SAR202 cluster bacterium.
OC   Bacteria; Chloroflexota; SAR202 cluster.
OX   NCBI_TaxID=2030829 {ECO:0000313|EMBL:PCI17304.1, ECO:0000313|Proteomes:UP000217661};
RN   [1] {ECO:0000313|Proteomes:UP000217661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCI17304.1}.
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DR   EMBL; NVSQ01000032; PCI17304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4S850; -.
DR   Proteomes; UP000217661; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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;
FT   DOMAIN          4..171
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   UNSURE          292
FT                   /note="D or N"
FT                   /evidence="ECO:0000313|EMBL:PCI17304.1"
SQ   SEQUENCE   321 AA;  34572 MW;  F712CB5AC8CC4AC4 CRC64;
     MKEVTYVEAL MEAFTEEMRR DDKVFHLCGN HGPLAALIPE FGEERVRACP ISEEAYVGAG
     IGAAGSGFRP IISPGMMTFA FTAMDQIVNQ MAKIHYMFGG QAPFPLVFRA STGGGRSAAA
     QHSQSPHPMF MNLAGLKLIM PSTPYDAKGL MKSAIRDNNP VVFFEDQILA ASPTKQEIPD
     EEYTVPIGVA DVKRQGRDVT VIAISKMVSH ALAAAEELAG QGIDVEVVDP RTLVPMDVPA
     LRASVQKTGR VVIVDEACLT CSAAAEISAL ITEDPATFRA LKAPPKRVCS PDVPIPYSPI
     MEQFCLPDKD NVIQGIREVL G
//