ID   ODP2_MYCBO              Reviewed;         553 AA.
AC   P65634; A0A1R3Y0P9; Q10381; X2BJM2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   28-JAN-2026, entry version 124.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex;
DE            EC=2.3.1.12;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2;
DE            Short=PDH component E2;
GN   Name=dlaT; Synonyms=sucB; OrderedLocusNames=BQ2027_MB2238;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA =
CC         N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 2 lipoyl cofactors covalently. {ECO:0000250};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. Part of the PDH complex, consisting of multiple copies of
CC       AceE (E1), DlaT (E2) and Lpd (E3). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIU00846.1; -; Genomic_DNA.
DR   RefSeq; WP_003411450.1; NC_002945.4.
DR   AlphaFoldDB; P65634; -.
DR   SMR; P65634; -.
DR   KEGG; mbo:BQ2027_MB2238; -.
DR   PATRIC; fig|233413.5.peg.2454; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031405; F:lipoic acid binding; IEA:TreeGrafter.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   FunFam; 2.40.50.100:FF:000023; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; 1.
DR   FunFam; 3.30.559.10:FF:000039; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; 1.
DR   FunFam; 4.10.320.10:FF:000008; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; 1.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR050743; 2-oxoacid_DH_E2_comp.
DR   InterPro; IPR014276; 2-oxoglutarate_DH_E2.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR02927; SucB_Actino; 1.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipoyl; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..553
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of pyruvate dehydrogenase complex"
FT                   /id="PRO_0000162267"
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          121..196
FT                   /note="Lipoyl-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          243..280
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   REGION          81..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..100
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..110
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..232
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..300
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        523
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        527
FT                   /evidence="ECO:0000250"
FT   MOD_RES         43
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         162
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ   SEQUENCE   553 AA;  57088 MW;  54B6E70D23B804A7 CRC64;
     MAFSVQMPAL GESVTEGTVT RWLKQEGDTV ELDEPLVEVS TDKVDTEIPS PAAGVLTKII
     AQEDDTVEVG GELAVIGDAK DAGEAAAPAP EKVPAAQPES KPAPEPPPVQ PTSGAPAGGD
     AKPVLMPELG ESVTEGTVIR WLKKIGDSVQ VDEPLVEVST DKVDTEIPSP VAGVLVSISA
     DEDATVPVGG ELARIGVAAD IGAAPAPKPA PKPVPEPAPT PKAEPAPSPP AAQPAGAAEG
     APYVTPLVRK LASENNIDLA GVTGTGVGGR IRKQDVLAAA EQKKRAKAPA PAAQAAAAPA
     PKAPPAPAPA LAHLRGTTQK ASRIRQITAN KTRESLQATA QLTQTHEVDM TKIVGLRARA
     KAAFAEREGV NLTFLPFFAK AVIDALKIHP NINASYNEDT KEITYYDAEH LGFAVDTEQG
     LLSPVIHDAG DLSLAGLARA IADIAARARS GNLKPDELSG GTFTITNIGS QGALFDTPIL
     VPPQAAMLGT GAIVKRPRVV VDASGNESIG VRSVCYLPLT YDHRLIDGAD AGRFLTTIKH
     RLEEGAFEAD LGL
//