ID   A0A1K1T395_9PSEU        Unreviewed;       769 AA.
AC   A0A1K1T395;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172};
GN   ORFNames=SAMN04489730_7821 {ECO:0000313|EMBL:SFW91105.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW91105.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW91105.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW91105.1,
RC   ECO:0000313|Proteomes:UP000182740};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00043719};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR000156-1};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; FPJG01000006; SFW91105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1T395; -.
DR   STRING; 546364.SAMN04489730_7821; -.
DR   Proteomes; UP000182740; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF4; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Pyruvate {ECO:0000313|EMBL:SFW91105.1}.
FT   DOMAIN          405..609
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         195
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ   SEQUENCE   769 AA;  82105 MW;  AB46BF3F51449847 CRC64;
     MTQASVTAPA TGSDELAAIE RRVLWLATAI VHHANRVRAN PSGLKVGGHQ ASCASLVSIM
     TSLWFRHLRP EDRVSVKPHA SPVLHAINYL LGELDEKYLT TLREFGGLQS YPSRAKDPDP
     VDYSTGSVGI GATAPIWGAL ARRYLTTRGS AAGTGRQYSL VGDAELDEGA IWEAILDPAV
     AELGEIVWIV DLNRQSLDRV VPNIAAGRLQ GMFDAAGWQV LTLKYGRLLE ELFTRPGGAE
     LRARIDAMPN PEYQRLLRCD AAQVRDRLPA GNAALASLVA SLDDETLLAA IRNLGGHDLG
     SLDEVFAAIS DDRPTVIFCY TVKGRGLPTQ GHPQNHSSLL TVSQMEELAA SLGTDLASPW
     ERFAPGSREA ELCAQAASRL RRPDVPSLPS VELPVDIGRT PSGTATTQAA LGRVLLDLTR
     EAPEAAKRVV TVSPDVSSTT NLGGWVNKVG VWSATERRDW FEDDPETIVH WREKPTGQHV
     ELGIAETNLV GLLGELGATW SRWGEPLLPI GVMYDPFVER ALEPWSFGIY AGGQSILIGT
     PSGVTLAPEG GAHQSITTPS IGVEQPGCVS YEPAFAIDTE WTLLAALGRL GKPGGTSSYF
     RLSTRPVDQT LAGVPADPAA RERRRRQVVA GAYLLRRAAE PAVTLAAMGA LVPDALAAAE
     RLAQVGVAAD VVCVTSPGLV FEALQARSGR GGGEPWILDQ VFPASRARPL VTVLDGHPHT
     LAFLAGINRV PSVALGVTRF GQSGSIEDVY RYHGIDTDSI IRAALDVLA
//