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P19262

- ODO2_YEAST

UniProt

P19262 - ODO2_YEAST

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

KGD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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).

    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 sitei435 – 4351By similarity
    Active sitei439 – 4391By similarity

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: SGD
    2. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    3. mitochondrial genome maintenance Source: SGD
    4. tricarboxylic acid cycle Source: SGD

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciYEAST:YDR148C-MONOMER.
    BRENDAi2.3.1.61. 984.
    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    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
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    Gene namesi
    Name:KGD2
    Ordered Locus Names:YDR148C
    ORF Names:YD8358.05C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR148c.
    SGDiS000002555. KGD2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial nucleoid Source: SGD
    2. mitochondrial oxoglutarate dehydrogenase complex Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 463Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020478
    Transit peptidei1 – ?Mitochondrion

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141N6-lipoyllysineSequence Analysis
    Modified residuei340 – 3401Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP19262.
    PaxDbiP19262.
    PeptideAtlasiP19262.
    PRIDEiP19262.

    Expressioni

    Inductioni

    Transcriptionally regulated by glucose and activated by the HAP2 and HAP3 proteins.

    Gene expression databases

    GenevestigatoriP19262.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YMR31P199553EBI-12464,EBI-16295

    Protein-protein interaction databases

    BioGridi32202. 171 interactions.
    DIPiDIP-1102N.
    IntActiP19262. 27 interactions.
    MINTiMINT-390263.
    STRINGi4932.YDR148C.

    Structurei

    3D structure databases

    ProteinModelPortaliP19262.
    SMRiP19262. Positions 73-150, 233-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini74 – 14774Lipoyl-bindingAdd
    BLAST
    Repeati185 – 19061
    Repeati191 – 19662
    Repeati197 – 20263
    Repeati204 – 20964; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 209254 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-[AV]Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115255.
    HOGENOMiHOG000281563.
    KOiK00658.
    OMAiIMPITIA.
    OrthoDBiEOG73V6W0.

    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.

    P19262-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSRATRTAA AKSLVKSKVA RNVMAASFVK RHASTSLFKQ ANKVESLGSI    50
    YLSGKKISVA ANPFSITSNR FKSTSIEVPP MAESLTEGSL KEYTKNVGDF 100
    IKEDELLATI ETDKIDIEVN SPVSGTVTKL NFKPEDTVTV GEELAQVEPG 150
    EAPAEGSGES KPEPTEQAEP SQGVAARENS SEETASKKEA APKKEAAPKK 200
    EVTEPKKADQ PKKTVSKAQE PPVASNSFTP FPRTETRVKM NRMRLRIAER 250
    LKESQNTAAS LTTFNEVDMS ALMEMRKLYK DEIIKKTGTK FGFMGLFSKA 300
    CTLAAKDIPA VNGAIEGDQI VYRDYTDISV AVATPKGLVT PVVRNAESLS 350
    VLDIENEIVR LSHKARDGKL TLEDMTGGTF TISNGGVFGS LYGTPIINSP 400
    QTAVLGLHGV KERPVTVNGQ IVSRPMMYLA LTYDHRLLDG REAVTFLKTV 450
    KELIEDPRKM LLW 463
    Length:463
    Mass (Da):50,431
    Last modified:February 1, 1996 - v2
    Checksum:iC06FEB1DE385AE19
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti170 – 20839PSQGV…EPKKA → HRKVSPQGKTQVRKRLQRKK LLQRKKPLQRKKLQNQKRT in AAA34720. (PubMed:2115121)CuratedAdd
    BLAST
    Sequence conflicti441 – 4455REAVT → EKLLS in AAA34720. (PubMed:2115121)Curated
    Sequence conflicti460 – 4634MLLW → CCYGDLKFAAHTNLIS in AAA34720. (PubMed:2115121)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34531 Genomic DNA. Translation: AAA34720.1.
    Z50046 Genomic DNA. Translation: CAA90371.1.
    BK006938 Genomic DNA. Translation: DAA11991.1.
    PIRiS57975. XUBYSD.
    RefSeqiNP_010432.3. NM_001180455.3.

    Genome annotation databases

    EnsemblFungiiYDR148C; YDR148C; YDR148C.
    GeneIDi851726.
    KEGGisce:YDR148C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34531 Genomic DNA. Translation: AAA34720.1 .
    Z50046 Genomic DNA. Translation: CAA90371.1 .
    BK006938 Genomic DNA. Translation: DAA11991.1 .
    PIRi S57975. XUBYSD.
    RefSeqi NP_010432.3. NM_001180455.3.

    3D structure databases

    ProteinModelPortali P19262.
    SMRi P19262. Positions 73-150, 233-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32202. 171 interactions.
    DIPi DIP-1102N.
    IntActi P19262. 27 interactions.
    MINTi MINT-390263.
    STRINGi 4932.YDR148C.

    Proteomic databases

    MaxQBi P19262.
    PaxDbi P19262.
    PeptideAtlasi P19262.
    PRIDEi P19262.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR148C ; YDR148C ; YDR148C .
    GeneIDi 851726.
    KEGGi sce:YDR148C.

    Organism-specific databases

    CYGDi YDR148c.
    SGDi S000002555. KGD2.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115255.
    HOGENOMi HOG000281563.
    KOi K00658.
    OMAi IMPITIA.
    OrthoDBi EOG73V6W0.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BioCyci YEAST:YDR148C-MONOMER.
    BRENDAi 2.3.1.61. 984.

    Miscellaneous databases

    NextBioi 969442.
    PROi P19262.

    Gene expression databases

    Genevestigatori P19262.

    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. "Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase."
      Repetto B., Tzagoloff A.
      Mol. Cell. Biol. 10:4221-4232(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
      Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
      Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.

    Entry informationi

    Entry nameiODO2_YEAST
    AccessioniPrimary (citable) accession number: P19262
    Secondary accession number(s): D6VSD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7970 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3