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P49367

- LYS4_YEAST

UniProt

P49367 - LYS4_YEAST

Protein

Homoaconitase, mitochondrial

Gene

LYS4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.2 Publications

    Catalytic activityi

    (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O.

    Cofactori

    Binds 1 4Fe-4S cluster per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi340 – 3401Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi407 – 4071Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi410 – 4101Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: InterPro
    2. homoaconitate hydratase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. lysine biosynthetic process via aminoadipic acid Source: SGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YDR234W-MONOMER.
    UniPathwayiUPA00033; UER01027.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homoaconitase, mitochondrial (EC:4.2.1.36)
    Alternative name(s):
    Homoaconitate hydratase
    Gene namesi
    Name:LYS4
    Synonyms:LYS3
    Ordered Locus Names:YDR234W
    ORF Names:YD8419.01, YD9934.18
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR234w.
    SGDiS000002642. LYS4.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2020MitochondrionSequence AnalysisAdd
    BLAST
    Chaini21 – 693673Homoaconitase, mitochondrialPRO_0000000551Add
    BLAST

    Proteomic databases

    MaxQBiP49367.
    PaxDbiP49367.
    PeptideAtlasiP49367.

    Expressioni

    Gene expression databases

    GenevestigatoriP49367.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399402EBI-10276,EBI-16219

    Protein-protein interaction databases

    BioGridi32285. 25 interactions.
    IntActiP49367. 1 interaction.
    MINTiMINT-2732625.
    STRINGi4932.YDR234W.

    Structurei

    3D structure databases

    ProteinModelPortaliP49367.
    SMRiP49367. Positions 23-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aconitase/IPM isomerase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1048.
    GeneTreeiENSGT00730000114222.
    HOGENOMiHOG000173778.
    KOiK01705.
    OMAiSWPVATK.
    OrthoDBiEOG70CRGK.

    Family and domain databases

    Gene3Di3.20.19.10. 1 hit.
    3.30.499.10. 2 hits.
    3.40.1060.10. 1 hit.
    InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
    IPR015937. Acoase/IPM_deHydtase.
    IPR001030. Acoase/IPM_deHydtase_lsu_aba.
    IPR015928. Aconitase/3IPM_dehydase_swvl.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
    IPR004418. Homoaconitase_mito.
    [Graphical view]
    PANTHERiPTHR11670. PTHR11670. 1 hit.
    PTHR11670:SF8. PTHR11670:SF8. 1 hit.
    PfamiPF00330. Aconitase. 2 hits.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00415. ACONITASE.
    SUPFAMiSSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 1 hit.
    TIGRFAMsiTIGR00139. h_aconitase. 1 hit.
    PROSITEiPS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49367-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRSTTFTRS FHSSRAWLKG QNLTEKIVQS YAVNLPEGKV VHSGDYVSIK    50
    PAHCMSHDNS WPVALKFMGL GATKIKNPSQ IVTTLDHDIQ NKSEKNLTKY 100
    KNIENFAKKH HIDHYPAGRG IGHQIMIEEG YAFPLNMTVA SDSHSNTYGG 150
    LGSLGTPIVR TDAAAIWATG QTWWQIPPVA QVELKGQLPQ GVSGKDIIVA 200
    LCGLFNNDQV LNHAIEFTGD SLNALPIDHR LTIANMTTEW GALSGLFPVD 250
    KTLIDWYKNR LQKLGTNNHP RINPKTIRAL EEKAKIPKAD KDAHYAKKLI 300
    IDLATLTHYV SGPNSVKVSN TVQDLSQQDI KINKAYLVSC TNSRLSDLQS 350
    AADVVCPTGD LNKVNKVAPG VEFYVAAASS EIEADARKSG AWEKLLKAGC 400
    IPLPSGCGPC IGLGAGLLEP GEVGISATNR NFKGRMGSKD ALAYLASPAV 450
    VAASAVLGKI SSPAEVLSTS EIPFSGVKTE IIENPVVEEE VNAQTEAPKQ 500
    SVEILEGFPR EFSGELVLCD ADNINTDGIY PGKYTYQDDV PKEKMAQVCM 550
    ENYDAEFRTK VHPGDIVVSG FNFGTGSSRE QAATALLAKG INLVVSGSFG 600
    NIFSRNSINN ALLTLEIPAL IKKLREKYQG APKELTRRTG WFLKWDVADA 650
    KVVVTEGSLD GPVILEQKVG ELGKNLQEII VKGGLEGWVK SQL 693
    Length:693
    Mass (Da):75,151
    Last modified:February 1, 1996 - v1
    Checksum:i9342E3CF83FE3FD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti581 – 5811Q → R in AAU09698. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46154 Genomic DNA. Translation: AAA88902.1.
    X93502 Genomic DNA. Translation: CAA63764.1.
    Z48612 Genomic DNA. Translation: CAA88513.1.
    Z49701 Genomic DNA. Translation: CAA89720.1.
    AY723781 Genomic DNA. Translation: AAU09698.1.
    BK006938 Genomic DNA. Translation: DAA12075.1.
    PIRiS61067.
    RefSeqiNP_010520.3. NM_001180542.3.

    Genome annotation databases

    EnsemblFungiiYDR234W; YDR234W; YDR234W.
    GeneIDi851820.
    KEGGisce:YDR234W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46154 Genomic DNA. Translation: AAA88902.1 .
    X93502 Genomic DNA. Translation: CAA63764.1 .
    Z48612 Genomic DNA. Translation: CAA88513.1 .
    Z49701 Genomic DNA. Translation: CAA89720.1 .
    AY723781 Genomic DNA. Translation: AAU09698.1 .
    BK006938 Genomic DNA. Translation: DAA12075.1 .
    PIRi S61067.
    RefSeqi NP_010520.3. NM_001180542.3.

    3D structure databases

    ProteinModelPortali P49367.
    SMRi P49367. Positions 23-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32285. 25 interactions.
    IntActi P49367. 1 interaction.
    MINTi MINT-2732625.
    STRINGi 4932.YDR234W.

    Proteomic databases

    MaxQBi P49367.
    PaxDbi P49367.
    PeptideAtlasi P49367.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR234W ; YDR234W ; YDR234W .
    GeneIDi 851820.
    KEGGi sce:YDR234W.

    Organism-specific databases

    CYGDi YDR234w.
    SGDi S000002642. LYS4.

    Phylogenomic databases

    eggNOGi COG1048.
    GeneTreei ENSGT00730000114222.
    HOGENOMi HOG000173778.
    KOi K01705.
    OMAi SWPVATK.
    OrthoDBi EOG70CRGK.

    Enzyme and pathway databases

    UniPathwayi UPA00033 ; UER01027 .
    BioCyci YEAST:YDR234W-MONOMER.

    Miscellaneous databases

    NextBioi 969689.

    Gene expression databases

    Genevestigatori P49367.

    Family and domain databases

    Gene3Di 3.20.19.10. 1 hit.
    3.30.499.10. 2 hits.
    3.40.1060.10. 1 hit.
    InterProi IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
    IPR015937. Acoase/IPM_deHydtase.
    IPR001030. Acoase/IPM_deHydtase_lsu_aba.
    IPR015928. Aconitase/3IPM_dehydase_swvl.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
    IPR004418. Homoaconitase_mito.
    [Graphical view ]
    PANTHERi PTHR11670. PTHR11670. 1 hit.
    PTHR11670:SF8. PTHR11670:SF8. 1 hit.
    Pfami PF00330. Aconitase. 2 hits.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00415. ACONITASE.
    SUPFAMi SSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 1 hit.
    TIGRFAMsi TIGR00139. h_aconitase. 1 hit.
    PROSITEi PS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms."
      Irvin S.D., Bhattacharjee J.K.
      J. Mol. Evol. 46:401-408(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Gamonet F., Lauquin G.J.-M.
      Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / GRF88.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Cloning and physical characterization of linked lysine genes (lys4, lys15) of Saccharomyces cerevisiae."
      Wang L., Okamoto S., Bhattacharjee J.K.
      Curr. Genet. 16:7-12(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "The fungal alpha-aminoadipate pathway for lysine biosynthesis requires two enzymes of the aconitase family for the isomerization of homocitrate to homoisocitrate."
      Fazius F., Shelest E., Gebhardt P., Brock M.
      Mol. Microbiol. 86:1508-1530(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiLYS4_YEAST
    AccessioniPrimary (citable) accession number: P49367
    Secondary accession number(s): D6VSL5, Q66RF2, Q7LH77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7350 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