ID   Q9CBS8_MYCLE            Unreviewed;       936 AA.
AC   Q9CBS8;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN   Name=aceE {ECO:0000313|EMBL:CAC30602.1};
GN   OrderedLocusNames=ML1651 {ECO:0000313|EMBL:CAC30602.1};
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC30602.1, ECO:0000313|Proteomes:UP000000806};
RN   [1] {ECO:0000313|EMBL:CAC30602.1, ECO:0000313|Proteomes:UP000000806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN {ECO:0000313|EMBL:CAC30602.1,
RC   ECO:0000313|Proteomes:UP000000806};
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC       catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|PIRNR:PIRNR000156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)-
CC         [(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00051231,
CC         ECO:0000256|PIRNR:PIRNR000156};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|PIRNR:PIRNR000156};
CC   -!- SUBUNIT: Homodimer. Part of the PDH complex, consisting of multiple
CC       copies of AceE (E1), DlaT (E2) and Lpd (E3).
CC       {ECO:0000256|ARBA:ARBA00063557}.
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DR   EMBL; AL583922; CAC30602.1; -; Genomic_DNA.
DR   PIR; E87115; E87115.
DR   RefSeq; WP_010908453.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBS8; -.
DR   STRING; 272631.gene:17575494; -.
DR   KEGG; mle:ML1651; -.
DR   PATRIC; fig|272631.5.peg.3118; -.
DR   Leproma; ML1651; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_11; -.
DR   OrthoDB; 9759664at2; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   FunFam; 3.40.50.970:FF:000011; Pyruvate dehydrogenase E1 component; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR051157; PDH/Transketolase.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR060495; PDH_E1_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR055152; Transketolase-like_C_2.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00759; aceE; 1.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF28598; PDH_E1_N; 1.
DR   Pfam; PF22613; Transketolase_C_1; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000156};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|PIRNR:PIRNR000156};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000806};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|PIRNR:PIRNR000156}.
FT   DOMAIN          38..80
FT                   /note="Pyruvate dehydrogenase E1 component N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF28598"
FT   DOMAIN          165..331
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          512..733
FT                   /note="Pyruvate dehydrogenase E1 component middle"
FT                   /evidence="ECO:0000259|Pfam:PF17831"
FT   DOMAIN          750..883
FT                   /note="Transketolase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22613"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..10
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..936
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ   SEQUENCE   936 AA;  104702 MW;  253544F17332DF17 CRC64;
     MTIEFARPDL AKNPSSTNES NSVRVIREGV ASYLPDIDPE ETAEWLESFD ELLKHSGPSR
     ARYLILRLLE RAGEQRVTIP ALTWTDYVNT IPTELEPWFP GDEDIERRYR TWIRWNAAIM
     VHRAQRPGVG VGGHISTYAS SAALYEVGFN HFFRGKSHPS GGDQVFIQGH ASPGIYARAF
     LEGRLSADQL DGFRQEHSHP GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNRY
     LHDRGIKDTS DQHVWCFLGD GEMDEPESRG LAHVASLEDL DNLIFVINCN LQRLDGPVRG
     NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADRDGAL VDLMNATPDG DYQTYKANDG
     RFVRDHFFGR DPRTKALVEH MSDQEIWNLK RGGHDYRKVY ASYRAAVDHK GQPTVILAKT
     IKGYALGKHF ESRNATHQMK KLTLEDLKEF RDTQRIPISD TELEENPYLP PYYHPGPDSP
     EIRYLLDRRR ALGGFLPERR TKSGALTLPG RDTYAALKTG SGQQEVATTM AIVRTFKEVL
     RHKEVGPRIV PIIPDEARTF GMDSWFPSLK IYNHNGQLYT AVDAQLMLAY KESEVGQILH
     EGIDEAGSVG SFIAAGTSYS THNEPMIPIY IFYSMFGFQR TGDGLWAAAD QMARGFLLGA
     TAGRTTLTGE GLQHADGHSL LLAATNPAVV TYDPAFAYEI AYIVESGLTR MFGEDPENVF
     FYITVYNEPY PQPPEPENFD PDGVLRGMYR YYTAKEQRSN KAHILASGVS MPAALTAAEM
     LSTQWDVAAD VWSVTSWGEL NRDGMSIETA RLRYPDQPTS VPYVTQVLSE ARSDNAGPVI
     AVSDWMRAVP EQIRPWVPGT YVTLGTDGFG FSDTRTATRR YFNTDAESQV VAVLEALARD
     GEIDPSVPVA ATRQYQIDDV QAAPEQTSDP GPGVQN
//