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P65634 (ODP2_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name=PDH component E2
Gene names
Name:dlaT
Synonyms:sucB
Ordered Locus Names:Mb2238
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity.

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 2 lipoyl cofactors covalently By similarity.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. Part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3) By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 E3-binding domain.

Contains 2 lipoyl-binding domains.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162267

Regions

Domain1 – 7676Lipoyl-binding 1
Domain122 – 19574Lipoyl-binding 2
Domain241 – 27838E3-binding

Sites

Active site5231 By similarity
Active site5271 By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Potential
Modified residue1621N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
P65634 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 54B6E70D23B804A7

FASTA55357,088
        10         20         30         40         50         60 
MAFSVQMPAL GESVTEGTVT RWLKQEGDTV ELDEPLVEVS TDKVDTEIPS PAAGVLTKII 

        70         80         90        100        110        120 
AQEDDTVEVG GELAVIGDAK DAGEAAAPAP EKVPAAQPES KPAPEPPPVQ PTSGAPAGGD 

       130        140        150        160        170        180 
AKPVLMPELG ESVTEGTVIR WLKKIGDSVQ VDEPLVEVST DKVDTEIPSP VAGVLVSISA 

       190        200        210        220        230        240 
DEDATVPVGG ELARIGVAAD IGAAPAPKPA PKPVPEPAPT PKAEPAPSPP AAQPAGAAEG 

       250        260        270        280        290        300 
APYVTPLVRK LASENNIDLA GVTGTGVGGR IRKQDVLAAA EQKKRAKAPA PAAQAAAAPA 

       310        320        330        340        350        360 
PKAPPAPAPA LAHLRGTTQK ASRIRQITAN KTRESLQATA QLTQTHEVDM TKIVGLRARA 

       370        380        390        400        410        420 
KAAFAEREGV NLTFLPFFAK AVIDALKIHP NINASYNEDT KEITYYDAEH LGFAVDTEQG 

       430        440        450        460        470        480 
LLSPVIHDAG DLSLAGLARA IADIAARARS GNLKPDELSG GTFTITNIGS QGALFDTPIL 

       490        500        510        520        530        540 
VPPQAAMLGT GAIVKRPRVV VDASGNESIG VRSVCYLPLT YDHRLIDGAD AGRFLTTIKH 

       550 
RLEEGAFEAD LGL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248341 Genomic DNA. Translation: CAD97091.1.
RefSeqNP_855887.1. NC_002945.3.

3D structure databases

ProteinModelPortalP65634.
SMRP65634. Positions 3-195, 243-283, 322-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb2238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD97091; CAD97091; Mb2238.
GeneID1091362.
KEGGmbo:Mb2238.
PATRIC18006616. VBIMycBov88188_2454.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281564.
KOK00658.
OMAQEDETVE.
ProtClustDBPRK11855.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR014276. 2-oxoglutarate_DH_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR02927. SucB_Actino. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_MYCBO
AccessionPrimary (citable) accession number: P65634
Secondary accession number(s): Q10381
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 19, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families