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Protein

Anthranilate synthase component 1

Gene

TRP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Multifunctional tryptophan biosynthesis protein (TRP3), Anthranilate synthase component 1 (TRP2)
  2. Anthranilate phosphoribosyltransferase (TRP4)
  3. N-(5'-phosphoribosyl)anthranilate isomerase (TRP1)
  4. Multifunctional tryptophan biosynthesis protein (TRP3)
  5. Tryptophan synthase (TRP5)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651TryptophanBy similarity
Metal bindingi343 – 3431MagnesiumBy similarity
Binding sitei431 – 4311ChorismateBy similarity
Binding sitei452 – 4521ChorismateBy similarity
Binding sitei468 – 4681Chorismate; via amide nitrogenBy similarity
Metal bindingi481 – 4811MagnesiumBy similarity

GO - Molecular functioni

  • anthranilate synthase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • tryptophan biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-30.
UniPathwayiUPA00035; UER00040.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate synthase component 1 (EC:4.1.3.27)
Alternative name(s):
Anthranilate synthase component I
Gene namesi
Name:TRP2
Ordered Locus Names:YER090W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER090W.
SGDiS000000892. TRP2.

Subcellular locationi

GO - Cellular componenti

  • anthranilate synthase complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 507506Anthranilate synthase component 1PRO_0000154134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei223 – 2231PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00899.
PeptideAtlasiP00899.

PTM databases

iPTMnetiP00899.

Interactioni

Subunit structurei

Tetramer of two components I and two components II.

Binary interactionsi

WithEntry#Exp.IntActNotes
TRP3P009374EBI-19575,EBI-19585

Protein-protein interaction databases

BioGridi36835. 76 interactions.
DIPiDIP-542N.
IntActiP00899. 14 interactions.
MINTiMINT-533017.

Structurei

3D structure databases

ProteinModelPortaliP00899.
SMRiP00899. Positions 3-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 2823Tryptophan bindingBy similarity
Regioni316 – 3172Chorismate bindingBy similarity
Regioni466 – 4683Chorismate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00620000088738.
HOGENOMiHOG000025142.
InParanoidiP00899.
KOiK01657.
OMAiMLRASNP.
OrthoDBiEOG7BGHW7.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR005256. Anth_synth_I_PabB.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00564. trpE_most. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P00899-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASIKIQPD IDSLKQLQQQ NDDSSINMYP VYAYLPSLDL TPHVAYLKLA
60 70 80 90 100
QLNNPDRKES FLLESAKTNN ELDRYSFIGI SPRKTIKTGP TEGIETDPLE
110 120 130 140 150
ILEKEMSTFK VAENVPGLPK LSGGAIGYIS YDCVRYFEPK TRRPLKDVLR
160 170 180 190 200
LPEAYLMLCD TIIAFDNVFQ RFQIIHNINT NETSLEEGYQ AAAQIITDIV
210 220 230 240 250
SKLTDDSSPI PYPEQPPIKL NQTFESNVGK EGYENHVSTL KKHIKKGDII
260 270 280 290 300
QGVPSQRVAR PTSLHPFNIY RHLRTVNPSP YLFYIDCLDF QIIGASPELL
310 320 330 340 350
CKSDSKNRVI THPIAGTVKR GATTEEDDAL ADQLRGSLKD RAEHVMLVDL
360 370 380 390 400
ARNDINRICD PLTTSVDKLL TIQKFSHVQH LVSQVSGVLR PEKTRFDAFR
410 420 430 440 450
SIFPAGTVSG APKVRAMELI AELEGERRGV YAGAVGHWSY DGKTMDNCIA
460 470 480 490 500
LRTMVYKDGI AYLQAGGGIV YDSDEYDEYV ETMNKMMANH STIVQAEELW

ADIVGSA
Length:507
Mass (Da):56,768
Last modified:January 23, 2007 - v4
Checksum:iFCC179C481DB3107
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2129TDDSSPIPY → DRRFLANTI in AAA35175 (PubMed:6323449).Curated
Sequence conflicti220 – 2201L → P (PubMed:6323449).Curated
Sequence conflicti223 – 23816TFESN…ENHVS → LLNRMWARKVTKITSP (PubMed:6323449).CuratedAdd
BLAST
Sequence conflicti262 – 2687TSLHPFN → SRYILSIFTD in AAA35175 (PubMed:6323449).Curated
Sequence conflicti276 – 2761V → I in AAA35175 (PubMed:6323449).Curated
Sequence conflicti323 – 3231T → A in AAA35175 (PubMed:6323449).Curated
Sequence conflicti330 – 3301L → G in AAA35175 (PubMed:6323449).Curated
Sequence conflicti401 – 4022SI → TN in AAA35175 (PubMed:6323449).Curated
Sequence conflicti461 – 50747AYLQA…IVGSA → LTCKLAVVLFTIQLSTMNML ETMNNDGQSQYYCASRRIVG RYRRISLKRAFSVFFPLDDI FIVFE (PubMed:6323449).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01388 Genomic DNA. Translation: AAA35175.1.
X68327 Genomic DNA. Translation: CAA48402.1.
U18839 Genomic DNA. Translation: AAB64645.1.
BK006939 Genomic DNA. Translation: DAA07751.1.
PIRiA49701. NNBY1.
RefSeqiNP_011014.1. NM_001178981.1.

Genome annotation databases

EnsemblFungiiYER090W; YER090W; YER090W.
GeneIDi856824.
KEGGisce:YER090W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01388 Genomic DNA. Translation: AAA35175.1.
X68327 Genomic DNA. Translation: CAA48402.1.
U18839 Genomic DNA. Translation: AAB64645.1.
BK006939 Genomic DNA. Translation: DAA07751.1.
PIRiA49701. NNBY1.
RefSeqiNP_011014.1. NM_001178981.1.

3D structure databases

ProteinModelPortaliP00899.
SMRiP00899. Positions 3-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36835. 76 interactions.
DIPiDIP-542N.
IntActiP00899. 14 interactions.
MINTiMINT-533017.

PTM databases

iPTMnetiP00899.

Proteomic databases

MaxQBiP00899.
PeptideAtlasiP00899.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER090W; YER090W; YER090W.
GeneIDi856824.
KEGGisce:YER090W.

Organism-specific databases

EuPathDBiFungiDB:YER090W.
SGDiS000000892. TRP2.

Phylogenomic databases

GeneTreeiENSGT00620000088738.
HOGENOMiHOG000025142.
InParanoidiP00899.
KOiK01657.
OMAiMLRASNP.
OrthoDBiEOG7BGHW7.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
BioCyciYEAST:MONOMER3O-30.

Miscellaneous databases

NextBioi983112.
PROiP00899.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR005256. Anth_synth_I_PabB.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00564. trpE_most. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288C / X2180-1A.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRPE_YEAST
AccessioniPrimary (citable) accession number: P00899
Secondary accession number(s): D3DLZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.