Anthranilate synthase component 1 - Saccharomyces cerevisiae (Baker's yeast)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P00899 (TRPE_YEAST)

Last modified February 9, 2010. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Anthranilate synthase component 1
    EC=4.1.3.27
Alternative name(s):
    Anthranilate synthase component I

Gene names

Name:	TRP2
Ordered Locus Names:	YER090W

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Hide | Top

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subunit structure	Tetramer of two components I and two components II.
Miscellaneous	Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity. Present with 6510 molecules/cell in log phase SD medium. Ref.5

Hide | Top

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	tryptophan biosynthetic process Ref.2 Inferred from mutant phenotype. Source: SGD
Cellular component	anthranilate synthase complex Inferred from physical interaction. Source: SGD
Molecular function	anthranilate synthase activity Ref.1 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
ARC40	P38328	1	EBI-19575,EBI-2777
ARO8	P53090	1	EBI-19575,EBI-2042933
BNA3	P47039	1	EBI-19575,EBI-25893
CYS4	P32582	1	EBI-19575,EBI-4167
GLN1	P32288	1	EBI-19575,EBI-7665
IPP1	P00817	1	EBI-19575,EBI-9338
OYE2	Q03558	1	EBI-19575,EBI-12729
RNR1	P21524	1	EBI-19575,EBI-15234
RNR2	P09938	1	EBI-19575,EBI-15240
SEC27	P41811	1	EBI-19575,EBI-4898
UBA1	P22515	1	EBI-19575,EBI-19703
VAS1	P07806-1	1	EBI-19575,EBI-1009942
VMA4	P22203	1	EBI-19575,EBI-20268

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 507

506

Anthranilate synthase component 1

PRO_0000154134

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

223

Phosphothreonine Ref.6

Experimental info

Sequence conflict

204 – 212

TDDSSPIPY → DRRFLANTI in AAA35175. Ref.1

Sequence conflict

220

L → P Ref.1

Sequence conflict

223 – 238

TFESN…ENHVS → LLNRMWARKVTKITSP Ref.1

Sequence conflict

262 – 268

TSLHPFN → SRYILSIFTD in AAA35175. Ref.1

Sequence conflict

276

V → I in AAA35175. Ref.1

Sequence conflict

323

T → A in AAA35175. Ref.1

Sequence conflict

330

L → G in AAA35175. Ref.1

Sequence conflict

401 – 402

SI → TN in AAA35175. Ref.1

Sequence conflict

461 – 507

AYLQA…IVGSA → LTCKLAVVLFTIQLSTMNML ETMNNDGQSQYYCASRRIVG RYRRISLKRAFSVFFPLDDI FIVFE Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P00899-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: FCC179C481DB3107
Show »

FASTA

507

56,768

        10         20         30         40         50         60 
MTASIKIQPD IDSLKQLQQQ NDDSSINMYP VYAYLPSLDL TPHVAYLKLA QLNNPDRKES 

        70         80         90        100        110        120 
FLLESAKTNN ELDRYSFIGI SPRKTIKTGP TEGIETDPLE ILEKEMSTFK VAENVPGLPK 

       130        140        150        160        170        180 
LSGGAIGYIS YDCVRYFEPK TRRPLKDVLR LPEAYLMLCD TIIAFDNVFQ RFQIIHNINT 

       190        200        210        220        230        240 
NETSLEEGYQ AAAQIITDIV SKLTDDSSPI PYPEQPPIKL NQTFESNVGK EGYENHVSTL 

       250        260        270        280        290        300 
KKHIKKGDII QGVPSQRVAR PTSLHPFNIY RHLRTVNPSP YLFYIDCLDF QIIGASPELL 

       310        320        330        340        350        360 
CKSDSKNRVI THPIAGTVKR GATTEEDDAL ADQLRGSLKD RAEHVMLVDL ARNDINRICD 

       370        380        390        400        410        420 
PLTTSVDKLL TIQKFSHVQH LVSQVSGVLR PEKTRFDAFR SIFPAGTVSG APKVRAMELI 

       430        440        450        460        470        480 
AELEGERRGV YAGAVGHWSY DGKTMDNCIA LRTMVYKDGI AYLQAGGGIV YDSDEYDEYV 

       490        500 
ETMNKMMANH STIVQAEELW ADIVGSA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3 encoding bifunctional anthranilate synthase: indole-3-glycerol phosphate synthase." Zalkin H., Paluh J.L., van Cleemput M., Moye W.S., Yanofsky C. J. Biol. Chem. 259:3985-3992(1984) [PubMed: 6323449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae." Graf R., Mehmann B., Braus G.H. J. Bacteriol. 175:1061-1068(1993) [PubMed: 8432699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288C / X2180-1A.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index." Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P., Perrot M. Yeast 11:601-613(1995) [PubMed: 7483834] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 2-16. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND THR-223, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	K01388 Genomic DNA. Translation: AAA35175.1. X68327 Genomic DNA. Translation: CAA48402.1. U18839 Genomic DNA. Translation: AAB64645.1.
PIR	NNBY1. A49701.
RefSeq	NP_011014.1.
3D structure databases
SMR	P00899. Positions 40-490.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-542N.
IntAct	P00899. 29 interactions.
STRING	P00899.
Proteomic databases
PeptideAtlas	P00899.
PRIDE	P00899.
Genome annotation databases
Ensembl	YER090W; YER090W; YER090W; Saccharomyces cerevisiae. [Genome view]
GeneID	856824.
KEGG	sce:YER090W.
NMPDR	fig\|4932.3.peg.2088.
Organism-specific databases
CYGD	YER090w.
SGD	S000000892. TRP2.
Phylogenomic databases
eggNOG	fuNOG04537.
HOGENOM	HBG507440.
OMA	VDEAYDD.
OrthoDB	EOG9GXH4B.
PhylomeDB	P00899.
Enzyme and pathway databases
BRENDA	4.1.3.27. 250.
Gene expression databases
ArrayExpress	P00899.
Genevestigator	P00899.
GermOnline	YER090W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005801. ADC_synthase. IPR006805. Anth_synth_I_N. IPR005256. Anth_synthI. IPR019999. Anthranilate_synth_I_C. IPR015890. Chorismate-bd_C. [Graphical view]
Gene3D	G3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.
PANTHER	PTHR11236. TRPE_1_chor_bd. 1 hit.
Pfam	PF04715. Anth_synt_I_N. 1 hit. PF00425. Chorismate_bind. 1 hit. [Graphical view]
PRINTS	PR00095. ANTSNTHASEI.
TIGRFAMs	TIGR00564. trpE_most. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	983112.

Hide | Top

Entry information

Entry name

TRPE_YEAST

Accession

Primary (citable) accession number: P00899

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents