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P20285 (ODP2_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 121. 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
MRP3
Pyruvate dehydrogenase complex component E2
Short name=PDC-E2
Short name=PDCE2
Gene names
Name:mrp-3
ORF Names:NCU07659
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). Ref.3

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subcellular location

Mitochondrion matrix.

Miscellaneous

The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Caution

Was originally (Ref.1) thought to be a ribosomal protein.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Ref.1
Chain29 – 458430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
PRO_0000020481

Regions

Domain35 – 10975Lipoyl-binding

Sites

Active site4311 Potential
Active site4351 Potential

Amino acid modifications

Modified residue751N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P20285 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 902A30C76ECA8149

FASTA45848,620
        10         20         30         40         50         60 
MIVPVLSRQA LRHASVARVA LPSLTRWYAS YPPHTVVKMP ALSPTMTSGG IGAWQKKPGD 

        70         80         90        100        110        120 
KIEPGEVLVE IETDKAQMDF EFQEEGVLAK ILKDSGEKDV AVGNPIAILV EEGTDVNAFK 

       130        140        150        160        170        180 
DFTLKDAGGE TSPAVPKDEP KNESTASAPT PAPTPAPEPE NTSFTGRFQT ALEREPNALP 

       190        200        210        220        230        240 
AAKRLAREKG IDLRNVKGSG PGGKITEEDV KKALASAPAA GAAAAAYTDV PISGMRKTIA 

       250        260        270        280        290        300 
ARLKESVTEN PHFFVSTNLS VSKLLKLRQA LNSSADGRYK LSVNDFLIKA MGIASKRVPT 

       310        320        330        340        350        360 
VNSSWRDGVI RQFETVDVSV AVATPNGLIT PIVKGVEGKG LESISAAVKE LAKKARDGKL 

       370        380        390        400        410        420 
KPEEYQGGSI SISNMGMNPA VQSFTAIINP PQAAILAVGA PQKVAVPVEN EDGTTGVSWD 

       430        440        450 
EQIIVTASFD HKVVDGAVGA EWIRELKKVI ENPLELLL 

« Hide

References

« Hide 'large scale' references
[1]"A mitochondrial protein from Neurospora crassa detected both on ribosomes and in membrane fractions. Analysis of the gene, the message, and the protein."
Kreader C.A., Langer C.S., Heckman J.E.
J. Biol. Chem. 264:317-327(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-50.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme."
Russel G.C., Guest J.R.
Biochim. Biophys. Acta 1076:225-232(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04432 Genomic DNA. Translation: AAA60452.1.
CM002239 Genomic DNA. Translation: EAA33550.1.
PIRA30775.
RefSeqXP_962786.1. XM_957693.2.
UniGeneNcr.16601.

3D structure databases

ProteinModelPortalP20285.
SMRP20285. Positions 28-122, 174-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU07659.1.

Proteomic databases

PRIDEP20285.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000007775; EFNCRP00000007764; EFNCRG00000007763.
GeneID3878934.
KEGGncr:NCU07659.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
KOK00627.
OMAKSTRISV.
OrthoDBEOG7TTQJ2.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR027189. LAT1_fungal.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR23151:SF24. PTHR23151:SF24. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_NEUCR
AccessionPrimary (citable) accession number: P20285
Secondary accession number(s): Q7RVH2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families