ID   A0A0T6AQ74_9BACT        Unreviewed;       341 AA.
AC   A0A0T6AQ74;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=XU14_C0026G0014 {ECO:0000313|EMBL:KRT76903.1};
OS   Armatimonadetes bacterium CSP1-3.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1640515 {ECO:0000313|EMBL:KRT76903.1, ECO:0000313|Proteomes:UP000051026};
RN   [1] {ECO:0000313|EMBL:KRT76903.1, ECO:0000313|Proteomes:UP000051026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-3 {ECO:0000313|EMBL:KRT76903.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) 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:KRT76903.1}.
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DR   EMBL; LDXQ01000026; KRT76903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6AQ74; -.
DR   PATRIC; fig|1640515.3.peg.1216; -.
DR   Proteomes; UP000051026; 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   Oxidoreductase {ECO:0000313|EMBL:KRT76903.1};
KW   Pyruvate {ECO:0000313|EMBL:KRT76903.1}.
FT   DOMAIN          19..194
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   341 AA;  36159 MW;  A91B34F1A8D10C37 CRC64;
     MSMPETAATP PATGAVREIT FGQAIREALA EEMRRDPRVF IIGEDVAEAG TPFKVLSGLV
     EEFGRERVID SPISEAGITG LATGAAMTGM RPVVDIMFGD FLTLAMDQIA NQAAKVHYMS
     GGKLKVPLVV RTTLGATRRS AAQHSQSLHA WVSHVPGLKV ALPSTPYDAK GLLKSAIRDD
     SPVVFFEDKM MYTMRGGVPA EEYTIPLGVA EVKRPGGDIT IVATSSMVHV ALAAAEALAA
     EGISAEVVDP RTTMPLDTET IIESARKTGR AMVVDEGYER YGVTAEIAAV IAEGAFQYLD
     APVRRLGAMH VPIPFSPVLE DLTVPTPETV AATARALCGR A
//