ID   A0A1A8ZE22_9ACTN        Unreviewed;       321 AA.
AC   A0A1A8ZE22;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=GA0070621_1455 {ECO:0000313|EMBL:SBT42250.1};
OS   Micromonospora narathiwatensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=299146 {ECO:0000313|EMBL:SBT42250.1, ECO:0000313|Proteomes:UP000198765};
RN   [1] {ECO:0000313|EMBL:SBT42250.1, ECO:0000313|Proteomes:UP000198765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45248 {ECO:0000313|EMBL:SBT42250.1,
RC   ECO:0000313|Proteomes:UP000198765};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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}.
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DR   EMBL; LT594324; SBT42250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8ZE22; -.
DR   PATRIC; fig|299146.4.peg.1507; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000198765; Chromosome i.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:SBT42250.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198765}.
FT   DOMAIN          4..177
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   321 AA;  34312 MW;  BF22A607542CA46E CRC64;
     MPRLSYRRAL TRALADEMTR DESVFLLGED IRVAAANVTS GLLKRFGPER VRDTPLSEQA
     FTSFATGAAL AGLRPVIEFQ IPSLLFLVFE QIVNHAHKFP LMTGGQCAVP VTYLVPGSGS
     RTGWAGQHSD HPYSLFAHVG VTTVVPATPA DAYGLLVSAI RCVDPVVVFA PAGAMDLRAD
     VTDLVPVPLG RGVVRRPGTD VTVVAVGHLV HDALAVAEEL ADQVSVEVFD PRTLYPFDRD
     GLVESVSRTG RLVVLDDSNR SCGIAGEIIA TVVERVRLAA PPRRVTRPDG AVLPFAPALD
     RAVQPGRDQL TAAIQLTMKD G
//