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O94681

- ODO2_SCHPO

UniProt

O94681 - ODO2_SCHPO

Protein

Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

kgd2

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 105 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei424 – 4241By similarity
    Active sitei428 – 4281By similarity

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: PomBase

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: PomBase
    2. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    3. tricarboxylic acid cycle Source: PomBase

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_208292. Lysine catabolism.
    REACT_213505. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2
    Short name:
    OGDC-E2
    Probable dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    Gene namesi
    Name:kgd2
    ORF Names:SPBC776.15c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC776.15c.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrial nucleoid Source: PomBase
    2. mitochondrial oxoglutarate dehydrogenase complex Source: PomBase
    3. mitochondrion Source: PomBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 452Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020477
    Transit peptidei1 – ?Mitochondrion

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831N6-lipoyllysineSequence Analysis

    Proteomic databases

    MaxQBiO94681.
    PaxDbiO94681.
    PRIDEiO94681.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4686150.
    STRINGi4896.SPBC776.15c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO94681.
    SMRiO94681. Positions 223-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 11674Lipoyl-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.
    HOGENOMiHOG000281563.
    KOiK00658.
    OMAiSMAESIT.
    OrthoDBiEOG73V6W0.
    PhylomeDBiO94681.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01347. sucB. 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.

    O94681-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSYGNGFRM MAKCLLSLRS GYSVTAPVSK SMANVLWARY ASTRIKTPPF    50
    PESITEGTLA QWLKQPGEYV NKDEEIASVE TDKIDAPVTA PDAGVLKEQL 100
    VKEGDTITID QDIAVIDTSA APPEGGSAGP KKDEVKTADA DAAKDLSTPQ 150
    DSSKPIEEKP MPDLGAEQKE SAPSSTKPAP DAKEPEFSSP KPKPAKSEPV 200
    KQSKPKATET ARPSSFSRNE DRVKMNRMRL RIAERLKESQ NRAASLTTFN 250
    ECDMSAVVAL RKKYKDEILK ETGVKIGFMS FFSKACTQAM KQIPAINGSI 300
    EGEGKGDTLV YRDFCDLSIA VATPKGLVTP VIRNAESMSL LEIESAIATL 350
    GSKARAGKLA IEDMASGTFT ISNGGIFGSL YGTPIINLPQ TAVLGLHAIK 400
    ERPVVINGQV VPRPMMYLAL TYDHRMVDGR EAVTFLRLVK EYIEDPAKML 450
    LV 452
    Length:452
    Mass (Da):48,964
    Last modified:May 1, 1999 - v1
    Checksum:iBAB03FB2842A37F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA22888.1.
    PIRiT40686.
    RefSeqiNP_596331.1. NM_001022252.2.

    Genome annotation databases

    EnsemblFungiiSPBC776.15c.1; SPBC776.15c.1:pep; SPBC776.15c.
    GeneIDi2541170.
    KEGGispo:SPBC776.15c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAA22888.1 .
    PIRi T40686.
    RefSeqi NP_596331.1. NM_001022252.2.

    3D structure databases

    ProteinModelPortali O94681.
    SMRi O94681. Positions 223-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4686150.
    STRINGi 4896.SPBC776.15c-1.

    Proteomic databases

    MaxQBi O94681.
    PaxDbi O94681.
    PRIDEi O94681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC776.15c.1 ; SPBC776.15c.1:pep ; SPBC776.15c .
    GeneIDi 2541170.
    KEGGi spo:SPBC776.15c.

    Organism-specific databases

    PomBasei SPBC776.15c.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281563.
    KOi K00658.
    OMAi SMAESIT.
    OrthoDBi EOG73V6W0.
    PhylomeDBi O94681.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    Reactomei REACT_208292. Lysine catabolism.
    REACT_213505. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    NextBioi 20802282.
    PROi O94681.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01347. sucB. 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 nameiODO2_SCHPO
    AccessioniPrimary (citable) accession number: O94681
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3