ID A0A221P6X8_9ACTN Unreviewed; 320 AA.
AC A0A221P6X8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=LK07_32845 {ECO:0000313|EMBL:ASN28011.1};
OS Streptomyces pluripotens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN28011.1, ECO:0000313|Proteomes:UP000031501};
RN [1] {ECO:0000313|EMBL:ASN28011.1, ECO:0000313|Proteomes:UP000031501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN28011.1,
RC ECO:0000313|Proteomes:UP000031501};
RA Ser H.-L., Lee L.-H.;
RT "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL Submitted (JUL-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}.
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DR EMBL; CP022433; ASN28011.1; -; Genomic_DNA.
DR RefSeq; WP_039649846.1; NZ_CP022433.1.
DR AlphaFoldDB; A0A221P6X8; -.
DR STRING; 1355015.LK06_031645; -.
DR KEGG; splu:LK06_031645; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000031501; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000031501}.
FT DOMAIN 4..177
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 320 AA; 33903 MW; 130BDBA4F8C86364 CRC64;
MTWLSYTKAL NRALADAMTE DDSVCVLGED VRAGMAGPTL GLHRRFGGER VLDMPLSEQA
FTSFAIGAAL SGMRPVVEFQ IPSLLFLVFE QIVNQAHKFR LMTGGQASIP VTFLVPGSGS
RTGWAGQHSD HPYSLFAHAG VKTAVPATPT DAYGLLRSAI AEDDPVVLFA PAGAMAARDD
VVGTPPPVPL GSGRIHRTGT DVTVVAVGHL VAHALSVADE LDGELSAEVL DPRTVHPVDW
ELLRASLRRT GRLVVYDDAN RACGFAAEVL AAAGEEAVLL APPRRVTRPD GAVLPFAPEL
DAALQPQPGQ LRDALRAVMR
//
