ODP2_MYCBO
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 25-MAY-2022, entry version 110.
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; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC 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=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC N(6)-(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; NP_855887.1; NC_002945.3.
DR RefSeq; WP_003411450.1; NC_002945.4.
DR AlphaFoldDB; P65634; -.
DR SMR; P65634; -.
DR EnsemblBacteria; SIU00846; SIU00846; BQ2027_MB2238.
DR PATRIC; fig|233413.5.peg.2454; -.
DR OMA; MKVPSPG; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
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 Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 2.
DR TIGRFAMs; TIGR02927; SucB_Actino; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Glycolysis; Lipoyl; 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 95..113
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 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
