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O59816

- ODP2_SCHPO

UniProt

O59816 - ODP2_SCHPO

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

lat1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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 sitei456 – 4561Sequence Analysis
    Active sitei460 – 4601Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: PomBase

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: PomBase

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_215777. Pyruvate metabolism.

    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
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDC-E2
    Short name:
    PDCE2
    Gene namesi
    Name:lat1
    ORF Names:SPCC794.07
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome III

    Organism-specific databases

    PomBaseiSPCC794.07.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial pyruvate dehydrogenase complex Source: PomBase
    2. mitochondrion Source: PomBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828MitochondrionBy similarityAdd
    BLAST
    Chaini29 – 483455Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000020482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei94 – 941N6-lipoyllysineBy similarity

    Proteomic databases

    MaxQBiO59816.
    PaxDbiO59816.

    Interactioni

    Protein-protein interaction databases

    BioGridi275378. 8 interactions.
    MINTiMINT-4676403.
    STRINGi4896.SPCC794.07-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO59816.
    SMRiO59816. Positions 58-134, 250-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 12875Lipoyl-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.
    PhylomeDBiO59816.

    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.

    O59816-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSANMLRRM HHGVAVTRML LVSNGKVQVK KSALYPVMAK LARTYATKNY    50
    PAHTVINMPA LSPTMTTGNI GAFQKKIGDK IEPGDVLCEI ETDKAQIDFE 100
    QQDEGYLAKI LIETGTKDVP VGKPLAVTVE NEGDVAAMAD FTIEDSSAKE 150
    PSAKSGEEKS APSSEKQSKE TSSPSNVSGE ERGDRVFASP LARKLAEEKD 200
    LDLSQIRGSG PNGRIIKVDI ENFKPVVAPK PSNEAAAKAT TPAASAADAA 250
    APGDYEDLPL SNMRKIIASR LAESKNMNPH YYVTVSVNME KIIRLRAALN 300
    AMADGRYKLS VNDLVIKATT AALRQVPEVN AAWMGDFIRQ YKNVDISMAV 350
    ATPSGLITPV IRNTHALGLA EISTLAKDYG QRARNNKLKP EEYQGGTFTI 400
    SNLGMFPVDQ FTAIINPPQA CILAVGTTVD TVVPDSTSEK GFKVAPIMKC 450
    TLSSDHRVVD GAMAARFTTA LKKILENPLE IML 483
    Length:483
    Mass (Da):52,061
    Last modified:August 1, 1998 - v1
    Checksum:i7E4B6340665932F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329672 Genomic DNA. Translation: CAA19134.1.
    PIRiT41615.
    RefSeqiNP_587755.1. NM_001022748.2.

    Genome annotation databases

    EnsemblFungiiSPCC794.07.1; SPCC794.07.1:pep; SPCC794.07.
    GeneIDi2538797.
    KEGGispo:SPCC794.07.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329672 Genomic DNA. Translation: CAA19134.1 .
    PIRi T41615.
    RefSeqi NP_587755.1. NM_001022748.2.

    3D structure databases

    ProteinModelPortali O59816.
    SMRi O59816. Positions 58-134, 250-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 275378. 8 interactions.
    MINTi MINT-4676403.
    STRINGi 4896.SPCC794.07-1.

    Proteomic databases

    MaxQBi O59816.
    PaxDbi O59816.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPCC794.07.1 ; SPCC794.07.1:pep ; SPCC794.07 .
    GeneIDi 2538797.
    KEGGi spo:SPCC794.07.

    Organism-specific databases

    PomBasei SPCC794.07.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    KOi K00627.
    OMAi MSMKEGT.
    OrthoDBi EOG7TTQJ2.
    PhylomeDBi O59816.

    Enzyme and pathway databases

    Reactomei REACT_215777. Pyruvate metabolism.

    Miscellaneous databases

    NextBioi 20799979.
    PROi O59816.

    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. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiODP2_SCHPO
    AccessioniPrimary (citable) accession number: O59816
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3