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P20285

- ODP2_NEUCR

UniProt

P20285 - ODP2_NEUCR

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

mrp-3

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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).

    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 – 4311Sequence Analysis
    Active sitei435 – 4351Sequence Analysis

    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

    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

    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-lipoyllysineBy similarity

    Proteomic databases

    PRIDEiP20285.

    Interactioni

    Protein-protein interaction databases

    STRINGi5141.NCU07659.1.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    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

    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: October 1, 2014
    This is version 124 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 thought to be a ribosomal protein.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3