ID   A0A286H7S5_9ACTN        Unreviewed;       777 AA.
AC   A0A286H7S5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172};
GN   ORFNames=SAMN06272739_4408 {ECO:0000313|EMBL:SOE03850.1};
OS   Blastococcus haudaquaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOE03850.1, ECO:0000313|Proteomes:UP000219482};
RN   [1] {ECO:0000313|Proteomes:UP000219482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2017) 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; OCNK01000008; SOE03850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286H7S5; -.
DR   Proteomes; UP000219482; 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; 2.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 2.
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:SOE03850.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219482}.
FT   DOMAIN          413..617
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   BINDING         168
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ   SEQUENCE   777 AA;  82605 MW;  A1AC3D21514364D6 CRC64;
     MSRTALHGDQ QTEHDRALRE IEQRVLWLAT SIVDHANRLR PNPTGLKVGG HQASSASMVT
     IMTALWLEQL DAQDRVSVKP HASPVLHALE YLLGQLDASY LPRLREFGGL QSYPSRLKDP
     VPADYSTGSV GIGATAPIWG ALARRYVGGH FGSGSTGGTG RQWSLVGDAE LDEGAVWETV
     LDPMVAELGE VVWVVDLNRQ SLDRVVPTMG ATRLQGMFAA AGWQVLTVKY GRLLEELFAR
     PGGEHLRARI DDMTNPEYQR MLRRTAAELR DALPGEGPAS GAIAGLIADV PDDDLRAAVR
     NLGGHDLTAL RTAFAQIDDT RPTVVLAYTL KGYGLATEGH PQNHSALLNE AQIAQLAEGL
     GVDPADPWAV LPAGSAAARL LTEAADRLRR VEEPPASAPE IPADLGRTPT GTATTQAALG
     RALLDLNRAA PEAGSRVVTV SPDVSSSTNL GGWVNKVGVW ASSERADWFA DDAETILHWR
     EQPSGQHIEL GIAETNLVGL MGELGTTWDR WGQPLLPIGV MYDPFVERAL EPWSFGIYAG
     GQSILVGTPS GVTLAAEGGA HQSIKTPSIG LEQPGCVTYE PAFVLDTEWC LLASLARLGR
     PGGSSAYLRL STRPIDQTLA AVPTDPAARE RRRRQVTAGA YALRRAGRPA VTLVAMGAVV
     PETLEAADRL AGLGIGADVV CVTSPGLLFR ALQARRGLDD AETWVLDTVF PRDRATPLVT
     VLDGHPHALA FLTGVNGVPG AHLGVTAFGQ SGDLASVYRF HGLDADSIVG AALDLVD
//