ID   B2HHR2_MYCMM            Unreviewed;       929 AA.
AC   B2HHR2;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   02-SEP-2026, entry version 96.
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:ACC41760.1};
GN   OrderedLocusNames=MMAR_3334 {ECO:0000313|EMBL:ACC41760.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41760.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC41760.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC41760.1; -; Genomic_DNA.
DR   RefSeq; WP_012394985.1; NC_010612.1.
DR   AlphaFoldDB; B2HHR2; -.
DR   STRING; 216594.MMAR_3334; -.
DR   KEGG; mmi:MMAR_3334; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_11; -.
DR   OrthoDB; 9759664at2; -.
DR   Proteomes; UP000001190; 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:000009; Pyruvate dehydrogenase E1 component; 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:UP000001190};
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          519..733
FT                   /note="Pyruvate dehydrogenase E1 component middle"
FT                   /evidence="ECO:0000259|Pfam:PF17831"
FT   DOMAIN          747..879
FT                   /note="Transketolase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22613"
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   929 AA;  103335 MW;  14244E526FF4C4F7 CRC64;
     MTTEFVRHDL AKTSSSASEP DRVRVIREGV ASYLPDIDPE ETSEWLESFD ALLEHSGPAR
     ARYLMLRLLE RAGEQRVAIP SLTSTDYVNT IPTELEPWFP GDEDVERRYR TWIRWNAAIM
     VHRAQRPGVG VGGHISTYAS SAALYEVGFN HFFRGKSHPG GGDQVFIQGH ASPGIYARAF
     LEGRLSADQL DGFRQEHSHP GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNHY
     LHDRGIKDTS DQHVWCFLGD GEMDEPESRG LAHMGALEGL DNLTFVINCN LQRLDGPVRG
     NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADRDGAL VNLMNSTPDG DYQTYKANDG
     AYVRDHFFGR DPRTKALVAN MSDQEIWNLK RGGHDYRKVY AAYRAAVDHK GQPTVILAKT
     IKGYSLGAHF QGRNATHQMK KLALADLKRF RDSMRIPVSD AQLDEDPYLP PYYHPGSDAP
     EIRYMLDRRR TLGGFLPERP TKAKTLTLPG PDAYKVLKKG SGQQEVATTM ALVRTFKELL
     RDKNIGNRIV PIIPDEARTF GMDSWFPSLK IYNRNGQLYT AVDAELMLAY KESHVGQILH
     EGINEAGSVG SFTAAGTSYA THNEPMIPIY IFYSMFGFQR TGDSFWAAAD QMARGFVLGA
     TAGRTTLTGE GLQHADGHSL LLAATNPAVV SYDPAFAYEL AYIIENGLSR MFGENPENIY
     FYITVYNEPY VQPAEPENFD PEGVLRGMYR YRAATKQCAH KAQLLASGVS MPDALKAAQM
     LADEWDVATD VWSVTSWSEL NRDGVSVERH RLRHPGEPAG VAYVTTALEG TSGPVVAVSD
     WMRAVPEQIR PWVPGTYVTL GTDGFGFSDT RPAARRYFNT DAESQVVAVL EALARDGEID
     ESVAVTAARQ YRIDDVQAAP KQTSDSGVA
//