ID   G8SD08_ACTS5            Unreviewed;       336 AA.
AC   G8SD08;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   OrderedLocusNames=ACPL_3123 {ECO:0000313|EMBL:AEV84018.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV84018.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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; CP003170; AEV84018.1; -; Genomic_DNA.
DR   RefSeq; WP_014690090.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8SD08; -.
DR   STRING; 134676.ACPL_3123; -.
DR   KEGG; ase:ACPL_3123; -.
DR   PATRIC; fig|134676.3.peg.3044; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   OrthoDB; 3512513at2; -.
DR   Proteomes; UP000005440; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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:AEV84018.1};
KW   Pyruvate {ECO:0000313|EMBL:AEV84018.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440}.
FT   DOMAIN          1..176
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   336 AA;  35814 MW;  2946EE9BD429658F CRC64;
     MIFAKELGDT LRGALGDDER VVLLGEDIAD PYGGAFKVTR GLSTAFPQRV RTTPISEGAI
     AGISAGLALA GYRPIAEVMF GDFLTLMFDQ VVNHIAKYQA MYAGQATCPV IVRAATGGHR
     GYGPTHSQSL EKHFLGVPHL RVVAASLYHD PRVVFADFLS RDEPVLYVEH KLLYPQHLTL
     PAGGMVGDLI ATADASPGML PTIRLSAVPV QDCTVSVLAY GYQAMLAARV IERLAIEEEI
     FAELVVPAQI APMDWAPVER SAAVTGSLVT VEEGADGWSW GSEAAAVMSR RLFGRLRRPV
     DVVASAPTVI PSSKVKEAEV LVGAARIEAA VRAAAR
//