Reviewed, UniProtKB/Swiss-Prot P32178 (CHMU_YEAST)

Names and origin

Protein names

Recommended name:
    Chorismate mutase
      Short name=CM
    EC=5.4.99.5

Gene names

Name:	ARO7
Synonyms:	OSM2
Ordered Locus Names:	YPR060C
ORF Names:	YP9499.15C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Chorismate = prephenate.
Enzyme regulation	Needs tryptophan for activation and tyrosine is a strong inhibitor. Allosterically regulated.
Pathway	Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subunit structure	Homodimer.
Sequence similarities	Contains 1 chorismate mutase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Molecular function	Isomerase
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	chorismate mutase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GLN1	P32288	1	EBI-4613,EBI-7665

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 256

256

Chorismate mutase

PRO_0000119204

Regions

Domain

3 – 255

253

Chorismate mutase

Experimental info

Mutagenesis

226

1

T → I: Constitutively activated and feedback-resistant. Ref.1

Secondary structure

1

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256

Helix Strand Turn

Details...

Helix

6 – 9

4

Helix

12 – 33

22

Helix

40 – 43

4

Beta strand

48 – 50

3

Helix

59 – 73

15

Helix

76 – 78

3

Turn

87 – 89

3

Helix

108 – 110

3

Helix

114 – 124

11

Helix

126 – 129

4

Beta strand

130 – 134

5

Helix

140 – 159

20

Helix

161 – 171

11

Helix

173 – 181

9

Helix

185 – 192

8

Helix

195 – 211

17

Beta strand

212 – 214

3

Helix

227 – 236

10

Helix

238 – 251

14

Turn

252 – 254

3

Sequences

	Sequence		Length	Mass (Da)
	P32178-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 8C6BEBEAA3497E23	FASTA	256	29,747
	10 20 30 40 50 60 MDFTKPETVL NLQNIRDELV RMEDSIIFKF IERSHFATCP SVYEANHPGL EIPNFKGSFL 70 80 90 100 110 120 DWALSNLEIA HSRIRRFESP DETPFFPDKI QKSFLPSINY PQILAPYAPE VNYNDKIKKV 130 140 150 160 170 180 YIEKIIPLIS KRDGDDKNNF GSVATRDIEC LQSLSRRIHF GKFVAEAKFQ SDIPLYTKLI 190 200 210 220 230 240 KSKDVEGIMK NITNSAVEEK ILERLTKKAE VYGVDPTNES GERRITPEYL VKIYKEIVIP 250 ITKEVEVEYL LRRLEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2646272] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 7971967] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"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: 8622937] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]	"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: 9384560] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M24517 Genomic DNA. Translation: AAB59309.1.
Z49219 Genomic DNA. Translation: CAA89177.1.
Z71255 Genomic DNA. Translation: CAA95004.1.
AY693179 Genomic DNA. Translation: AAT93198.1.

PIR

A45921.

RefSeq

NP_015385.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P32178. 4 interactions.

Proteomic databases

PeptideAtlas

P32178.

Genome annotation databases

Ensembl

YPR060C. Saccharomyces cerevisiae. [Contig view]

GeneID

856173.

GenomeReviews

Gene locus YPR060C in contig U00094_GR.

KEGG

sce:YPR060C.

NMPDR

fig|4932.3.peg.6521.

Organism-specific databases

CYGD

YPR060c.

SGD

S000006264. ARO7.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P32178.

OMA

P32178. SRRIHFG.

Enzyme and pathway databases

BRENDA

5.4.99.5. 250.

Gene expression databases

GermOnline

YPR060C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002701. Chorismate_mut.
IPR008238. Chorismate_mutase_AroQ_euk.
[Graphical view]

Gene3D

G3DSA:1.10.590.10. Chor_mut_AroQ_eu. 1 hit.

PANTHER

PTHR21145. Chor_mut_AroQ_eu. 1 hit.

Pfam

PF01817. CM_2. 1 hit.
[Graphical view]

PIRSF

PIRSF017318. Chor_mut_AroQ_eu. 1 hit.

TIGRFAMs

TIGR01802. CM_pl-yst. 1 hit.

PROSITE

PS51169. CHORISMATE_MUT_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981331.

Entry information

Entry name

CHMU_YEAST

Accession

Primary (citable) accession number: P32178

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)