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P32178

- CHMU_YEAST

UniProt

P32178 - CHMU_YEAST

Protein

Chorismate mutase

Gene

ARO7

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 130 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Chorismate = prephenate.

    Enzyme regulationi

    Needs tryptophan for activation and tyrosine is a strong inhibitor. Allosterically regulated.

    Pathwayi

    GO - Molecular functioni

    1. chorismate mutase activity Source: SGD

    GO - Biological processi

    1. chorismate metabolic process Source: InterPro
    2. L-phenylalanine biosynthetic process Source: SGD
    3. tyrosine biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Enzyme and pathway databases

    BioCyciYEAST:YPR060C-MONOMER.
    UniPathwayiUPA00120; UER00203.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chorismate mutase (EC:5.4.99.5)
    Short name:
    CM
    Gene namesi
    Name:ARO7
    Synonyms:OSM2
    Ordered Locus Names:YPR060C
    ORF Names:YP9499.15C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPR060c.
    SGDiS000006264. ARO7.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi226 – 2261T → I: Constitutively activated and feedback-resistant. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 256256Chorismate mutasePRO_0000119204Add
    BLAST

    Proteomic databases

    MaxQBiP32178.
    PaxDbiP32178.
    PeptideAtlasiP32178.

    Expressioni

    Gene expression databases

    GenevestigatoriP32178.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi36233. 112 interactions.
    IntActiP32178. 3 interactions.
    MINTiMINT-4506098.
    STRINGi4932.YPR060C.

    Structurei

    Secondary structure

    1
    256
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94
    Helixi12 – 3423
    Helixi40 – 423
    Beta strandi48 – 503
    Helixi59 – 7315
    Helixi76 – 783
    Turni87 – 893
    Helixi108 – 1103
    Helixi114 – 12411
    Helixi126 – 1294
    Beta strandi130 – 1345
    Helixi137 – 1393
    Helixi140 – 15920
    Helixi161 – 17010
    Helixi173 – 1819
    Helixi185 – 1917
    Helixi195 – 21117
    Beta strandi212 – 2143
    Helixi227 – 23610
    Helixi238 – 25114
    Turni252 – 2543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CSMX-ray2.20A/B1-256[»]
    2CSMX-ray2.80A1-256[»]
    3CSMX-ray3.00A/B1-256[»]
    4CSMX-ray2.80A/B1-256[»]
    5CSMX-ray2.00A1-256[»]
    ProteinModelPortaliP32178.
    SMRiP32178. Positions 1-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32178.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 255253Chorismate mutasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chorismate mutase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1605.
    HOGENOMiHOG000176992.
    KOiK01850.
    OMAiFEAVEEM.
    OrthoDBiEOG78PVMF.

    Family and domain databases

    Gene3Di1.10.590.10. 1 hit.
    InterProiIPR008238. Chorismate_mutase_AroQ_euk.
    IPR020822. Chorismate_mutase_type_II.
    [Graphical view]
    PANTHERiPTHR21145. PTHR21145. 1 hit.
    PfamiPF01817. CM_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017318. Chor_mut_AroQ_eu. 1 hit.
    SUPFAMiSSF48600. SSF48600. 1 hit.
    TIGRFAMsiTIGR01802. CM_pl-yst. 1 hit.
    PROSITEiPS51169. CHORISMATE_MUT_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32178-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDFTKPETVL NLQNIRDELV RMEDSIIFKF IERSHFATCP SVYEANHPGL    50
    EIPNFKGSFL DWALSNLEIA HSRIRRFESP DETPFFPDKI QKSFLPSINY 100
    PQILAPYAPE VNYNDKIKKV YIEKIIPLIS KRDGDDKNNF GSVATRDIEC 150
    LQSLSRRIHF GKFVAEAKFQ SDIPLYTKLI KSKDVEGIMK NITNSAVEEK 200
    ILERLTKKAE VYGVDPTNES GERRITPEYL VKIYKEIVIP ITKEVEVEYL 250
    LRRLEE 256
    Length:256
    Mass (Da):29,747
    Last modified:October 1, 1993 - v1
    Checksum:i8C6BEBEAA3497E23
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24517 Genomic DNA. Translation: AAB59309.1.
    Z49219 Genomic DNA. Translation: CAA89177.1.
    Z71255 Genomic DNA. Translation: CAA95004.1.
    AY693179 Genomic DNA. Translation: AAT93198.1.
    BK006949 Genomic DNA. Translation: DAA11481.1.
    PIRiA45921.
    RefSeqiNP_015385.1. NM_001184157.1.

    Genome annotation databases

    EnsemblFungiiYPR060C; YPR060C; YPR060C.
    GeneIDi856173.
    KEGGisce:YPR060C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24517 Genomic DNA. Translation: AAB59309.1 .
    Z49219 Genomic DNA. Translation: CAA89177.1 .
    Z71255 Genomic DNA. Translation: CAA95004.1 .
    AY693179 Genomic DNA. Translation: AAT93198.1 .
    BK006949 Genomic DNA. Translation: DAA11481.1 .
    PIRi A45921.
    RefSeqi NP_015385.1. NM_001184157.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CSM X-ray 2.20 A/B 1-256 [» ]
    2CSM X-ray 2.80 A 1-256 [» ]
    3CSM X-ray 3.00 A/B 1-256 [» ]
    4CSM X-ray 2.80 A/B 1-256 [» ]
    5CSM X-ray 2.00 A 1-256 [» ]
    ProteinModelPortali P32178.
    SMRi P32178. Positions 1-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36233. 112 interactions.
    IntActi P32178. 3 interactions.
    MINTi MINT-4506098.
    STRINGi 4932.YPR060C.

    Proteomic databases

    MaxQBi P32178.
    PaxDbi P32178.
    PeptideAtlasi P32178.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPR060C ; YPR060C ; YPR060C .
    GeneIDi 856173.
    KEGGi sce:YPR060C.

    Organism-specific databases

    CYGDi YPR060c.
    SGDi S000006264. ARO7.

    Phylogenomic databases

    eggNOGi COG1605.
    HOGENOMi HOG000176992.
    KOi K01850.
    OMAi FEAVEEM.
    OrthoDBi EOG78PVMF.

    Enzyme and pathway databases

    UniPathwayi UPA00120 ; UER00203 .
    BioCyci YEAST:YPR060C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32178.
    NextBioi 981331.

    Gene expression databases

    Genevestigatori P32178.

    Family and domain databases

    Gene3Di 1.10.590.10. 1 hit.
    InterProi IPR008238. Chorismate_mutase_AroQ_euk.
    IPR020822. Chorismate_mutase_type_II.
    [Graphical view ]
    PANTHERi PTHR21145. PTHR21145. 1 hit.
    Pfami PF01817. CM_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017318. Chor_mut_AroQ_eu. 1 hit.
    SUPFAMi SSF48600. SSF48600. 1 hit.
    TIGRFAMsi TIGR01802. CM_pl-yst. 1 hit.
    PROSITEi PS51169. CHORISMATE_MUT_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A single point mutation results in a constitutively activated and feedback-resistant chorismate mutase of Saccharomyces cerevisiae."
      Schmidheini T., Sperisen P., Paravicini G., Huetter R., Braus G.H.
      J. Bacteriol. 171:1245-1253(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF THR-226.
      Strain: ATCC 26109 / X2180.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "The crystal structure of allosteric chorismate mutase at 2.2-A resolution."
      Xue Y., Lipscomb W.N., Graf R., Schnappauf G., Braus G.
      Proc. Natl. Acad. Sci. U.S.A. 91:10814-10818(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    7. "Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state."
      Straeter N., Haakansson K., Schnappauf G., Braus G., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 93:3330-3334(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    8. "Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures."
      Straeter N., Schnappauf G., Braus G., Lipscomb W.N.
      Structure 5:1437-1452(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiCHMU_YEAST
    AccessioniPrimary (citable) accession number: P32178
    Secondary accession number(s): D6W465
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 130 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

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3