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P0CN86 (TRPG_CRYNJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multifunctional tryptophan biosynthesis protein

Including the following 3 domains:

  1. Anthranilate synthase component 2
    Short name=AS
    EC=4.1.3.27
    Alternative name(s):
    Anthranilate synthase, glutamine amidotransferase component
  2. Indole-3-glycerol phosphate synthase
    Short name=IGPS
    EC=4.1.1.48
  3. N-(5'-phosphoribosyl)anthranilate isomerase
    Short name=PRAI
    EC=5.3.1.24
Gene names
Name:TRP1
Ordered Locus Names:CNI00560
OrganismCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) [Reference proteome]
Taxonomic identifier214684 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities. HAMAP-Rule MF_00135

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00135

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00135

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. HAMAP-Rule MF_00135

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5. HAMAP-Rule MF_00135

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 752752Multifunctional tryptophan biosynthesis protein HAMAP-Rule MF_00135
PRO_0000056857

Regions

Domain3 – 202200Glutamine amidotransferase type-1
Region231 – 495265Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00135
Region509 – 752244N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135

Sites

Active site861For GATase activity By similarity
Active site1761For GATase activity By similarity
Active site1781For GATase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CN86 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: BE85651BED85BBE5

FASTA75280,473
        10         20         30         40         50         60 
MGFTLLIDNY DSFTWNIYAD LASVGGNPYV VRNDKITLKE IEGMFSDGEL ERIVISPGPG 

        70         80         90        100        110        120 
HPRTDSGVSR DVIAWGMGKL PILGVCMGLE CIVDLLGGEI AYAGEIKHGK TSLVQHDSIG 

       130        140        150        160        170        180 
VFHNLPQFLS STRYHSLSAQ IQSLPSVLQV TSTTKESGVI MGVRHRTYTV EAVQYHPESC 

       190        200        210        220        230        240 
MSEGGRGLMA NFIQMKGGKW GGENAWCGVP AEGEEEQPKA KTNGAPSLPT ILNRIHAQRL 

       250        260        270        280        290        300 
LDVEQAEKVP ATSPANVSTS LSLYASPPLI NFRDRMVSTP HTAVMAEIKR ASPSKGDIAP 

       310        320        330        340        350        360 
TASAPEQALK YALAGASVIS VLTEPTWFKG SLLDMLAVRN AVDSLPNRPA ILRKDFVLSK 

       370        380        390        400        410        420 
YMIDEARLYG ADTVLLIVAM LEPQQLKELY DYSVSLGMEP LVEVNNPTEL SLALEIGSKV 

       430        440        450        460        470        480 
IGVNNRNLHD FNVDMSTTSR VNAALNGRDV VLCALSGISS HEDVEKYVKE GVKGVLVGEA 

       490        500        510        520        530        540 
LMRASDTKAF LRSLIGLPPL EVVPKSRPLV KICGIRSTDD AKLAISAGAD LLGVILVPGT 

       550        560        570        580        590        600 
KRCISTSTAR EISALVQSAR SQSSSKPLEP SLSSPWFTTQ SDLLSSRRKP LLVGVFQNQS 

       610        620        630        640        650        660 
LSDILSAVEE IGLDLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE FRRPGLNQAI 

       670        680        690        700        710        720 
LLDAGGVSGG GGEGKAFPWE HAKRLIQSGE VGSEGHMPLP VILAGGLTPE NVGQAIEQAG 

       730        740        750 
EGVWCVDVSS GVEGEGGKVK EKVEAFVKAV RG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017349 Genomic DNA. Translation: AAW45488.1.
RefSeqXP_572795.1. XM_572795.1.
UniGeneFne.446.

3D structure databases

ProteinModelPortalP0CN86.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAW45488; AAW45488; CNI00560.
GeneID3259660.
KEGGcne:CNI00560.

Phylogenomic databases

KOK13501.
OrthoDBEOG78WM1Q.

Enzyme and pathway databases

UniPathwayUPA00035; UER00040.
UPA00035; UER00042.
UPA00035; UER00043.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR016302. Anthranilate_synth_II.
IPR017926. GATASE.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamPF00117. GATase. 1 hit.
PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
PIRSFPIRSF001382. TrpG-trpC-trpF. 1 hit.
SUPFAMSSF51366. SSF51366. 3 hits.
TIGRFAMsTIGR00566. trpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
PS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPG_CRYNJ
AccessionPrimary (citable) accession number: P0CN86
Secondary accession number(s): Q55NN6, Q5KC22
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: February 19, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways