Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0CN87 (TRPG_CRYNB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:CNBH0530
OrganismCryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) [Complete proteome]
Taxonomic identifier283643 [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_0000410098

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
P0CN87 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: BF1BCFE4462EBB7C

FASTA75280,438
        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 IGLNLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE IRRPGLNQAI 

       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
AAEY01000041 Genomic DNA. Translation: EAL19359.1.
RefSeqXP_774006.1. XM_768913.1.

3D structure databases

ProteinModelPortalP0CN87.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4937569.
KEGGcnb:CNBH0530.

Phylogenomic databases

KOK13501.
OrthoDBEOG78WM1Q.

Enzyme and pathway databases

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

Family and domain databases

Gene3D3.20.20.70. 2 hits.
3.40.50.880. 1 hit.
HAMAPMF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR016302. Anthranilate_synth_II.
IPR029062. Class_I_gatase-like.
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.
SSF52317. SSF52317. 1 hit.
TIGRFAMsTIGR00566. trpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
PS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPG_CRYNB
AccessionPrimary (citable) accession number: P0CN87
Secondary accession number(s): Q55NN6, Q5KC22
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 11, 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