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P20285

- ODP2_NEUCR

UniProt

P20285 - ODP2_NEUCR

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene
mrp-3, NCU07659
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei431 – 4311 Reviewed prediction
Active sitei435 – 4351 Reviewed prediction

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: EnsemblFungi
  2. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:mrp-3
ORF Names:NCU07659
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 4, Linkage Group IV

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828Mitochondrion1 PublicationAdd
BLAST
Chaini29 – 458430Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751N6-lipoyllysine By similarity

Proteomic databases

PRIDEiP20285.

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU07659.1.

Structurei

3D structure databases

ProteinModelPortaliP20285.
SMRiP20285. Positions 28-122, 174-212.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 10975Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiMSMKEGT.
OrthoDBiEOG7TTQJ2.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20285-1 [UniParc]FASTAAdd to Basket

« Hide

MIVPVLSRQA LRHASVARVA LPSLTRWYAS YPPHTVVKMP ALSPTMTSGG    50
IGAWQKKPGD KIEPGEVLVE IETDKAQMDF EFQEEGVLAK ILKDSGEKDV 100
AVGNPIAILV EEGTDVNAFK DFTLKDAGGE TSPAVPKDEP KNESTASAPT 150
PAPTPAPEPE NTSFTGRFQT ALEREPNALP AAKRLAREKG IDLRNVKGSG 200
PGGKITEEDV KKALASAPAA GAAAAAYTDV PISGMRKTIA ARLKESVTEN 250
PHFFVSTNLS VSKLLKLRQA LNSSADGRYK LSVNDFLIKA MGIASKRVPT 300
VNSSWRDGVI RQFETVDVSV AVATPNGLIT PIVKGVEGKG LESISAAVKE 350
LAKKARDGKL KPEEYQGGSI SISNMGMNPA VQSFTAIINP PQAAILAVGA 400
PQKVAVPVEN EDGTTGVSWD EQIIVTASFD HKVVDGAVGA EWIRELKKVI 450
ENPLELLL 458
Length:458
Mass (Da):48,620
Last modified:February 1, 1996 - v2
Checksum:i902A30C76ECA8149
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04432 Genomic DNA. Translation: AAA60452.1.
CM002239 Genomic DNA. Translation: EAA33550.1.
PIRiA30775.
RefSeqiXP_962786.1. XM_957693.2.
UniGeneiNcr.16601.

Genome annotation databases

EnsemblFungiiEFNCRT00000007775; EFNCRP00000007764; EFNCRG00000007763.
GeneIDi3878934.
KEGGincr:NCU07659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04432 Genomic DNA. Translation: AAA60452.1 .
CM002239 Genomic DNA. Translation: EAA33550.1 .
PIRi A30775.
RefSeqi XP_962786.1. XM_957693.2.
UniGenei Ncr.16601.

3D structure databases

ProteinModelPortali P20285.
SMRi P20285. Positions 28-122, 174-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU07659.1.

Proteomic databases

PRIDEi P20285.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000007775 ; EFNCRP00000007764 ; EFNCRG00000007763 .
GeneIDi 3878934.
KEGGi ncr:NCU07659.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
KOi K00627.
OMAi MSMKEGT.
OrthoDBi EOG7TTQJ2.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiODP2_NEUCR
AccessioniPrimary (citable) accession number: P20285
Secondary accession number(s): Q7RVH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Caution

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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