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P32178

- CHMU_YEAST

UniProt

P32178 - CHMU_YEAST

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Protein
Chorismate mutase
Gene
ARO7, OSM2, YPR060C, YP9499.15C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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 mutase
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP32178.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 255253Chorismate mutase
Add
BLAST

Sequence similaritiesi

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...

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

« Hide 'large scale' publications
  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: May 14, 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

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

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