ID   A0A0M9XA92_9ACTN        Unreviewed;       334 AA.
AC   A0A0M9XA92;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=ADK41_07665 {ECO:0000313|EMBL:KOT42668.1};
OS   Streptomyces caelestis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT42668.1, ECO:0000313|Proteomes:UP000037773};
RN   [1] {ECO:0000313|EMBL:KOT42668.1, ECO:0000313|Proteomes:UP000037773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT42668.1,
RC   ECO:0000313|Proteomes:UP000037773};
RA   Noorani M.;
RL   Submitted (JUL-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:KOT42668.1}.
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DR   EMBL; LGCN01000074; KOT42668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9XA92; -.
DR   PATRIC; fig|36816.3.peg.1649; -.
DR   Proteomes; UP000037773; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:KOT42668.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037773}.
FT   DOMAIN          14..189
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   334 AA;  35119 MW;  E42B9FE47A37090B CRC64;
     MTVGAGGGKG TGATTYREAM REALREALRS DDRVFLMGED VGRYGGCFGV SLGLLEEFGP
     ERVRDTPLSE SAFVGAGIGA ALAGMRPIVE IMTVNFSLLA LDQILNNAAT LLHMSGGQLP
     VPLVIRTTTG AGRQLAAQHS HSLEGWYAHI PGLRVLAPAT LEDARHMLAP ALADPDPVLI
     FEHGSLYNAS GELPPPTGPV DLDHAAVRRP GTDISLITYG GSLPKALAAA DELASGGISA
     EVIDLRTLRP LDQAVIASSV ARTHRAVVVD EAWRTGSLAA ELSARIAEES FYDLDAPVER
     VCSAEVPIPY ARRLEEAALP QTADVVAAVH RAVD
//