Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P86197 (ODP2_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 16. 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, mitochondrial

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name=PDC-E2
Short name=PDCE2
Gene names
Name:DLAT
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length219 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle By similarity. UniProtKB P08461

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. UniProtKB P08461

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. UniProtKB P08461

Subunit structure

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3 By similarity.

Subcellular location

Mitochondrion matrix By similarity UniProtKB P08461.

Tissue specificity

Detected at higher levels in cauda epididymal spermatazoa than in caput epididymal spermatazoa (at protein level). Ref.1

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 2 lipoyl-binding domains.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Tricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological_processglucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain‹1 – 219›219Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
PRO_0000394399

Regions

Domain‹1 – ›17›17Lipoyl-binding 1 UniProtKB P08461
Domain‹18 – 28›11Lipoyl-binding 2 UniProtKB P08461
Region37 – 5721E3- and/or E1-component binding domain Potential UniProtKB P08461
Region187 – 19812CoA-binding By similarity UniProtKB P08461

Sites

Active site1921 Potential UniProtKB P08461
Active site1961 Potential UniProtKB P08461

Amino acid modifications

Modified residue1211N6-succinyllysine By similarity

Experimental info

Non-adjacent residues17 – 182
Non-adjacent residues31 – 322
Non-adjacent residues40 – 412
Non-adjacent residues55 – 562
Non-adjacent residues63 – 642
Non-adjacent residues121 – 1222
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P86197 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 11B4C4C826FE3B08

FASTA21923,117
        10         20         30         40         50         60 
VPLPSLSPTM QAGTIARDVP LGAPLCIIVE KGRVFVSPLA KGIDLTQVKG TGPEGDIDSF 

        70         80         90        100        110        120 
VPSKVPEANS SWMDTVIRQN HVVDVSVAVS TPAGLITPIV FNAHIKGLET IASDVVSLAS 

       130        140        150        160        170        180 
KEGKLQPHEF QGGTFTISNL GMFGIKNFSA IINPPQACIL AIGASEDKLI PADNEKGFDV 

       190        200        210 
ASVMSVTLSC DHRVVDGAVG AQWLAEFKKY LEKPITMLL 

« Hide

References

[1]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP86197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_MESAU
AccessionPrimary (citable) accession number: P86197
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: March 19, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families