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Q92411 (TRPG_COCHE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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
OrganismCochliobolus heterostrophus (Southern corn leaf blight fungus) (Bipolaris maydis)
Taxonomic identifier5016 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeBipolaris

Protein attributes

Sequence length768 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 – 768768Multifunctional tryptophan biosynthesis protein HAMAP-Rule MF_00135
PRO_0000056856

Regions

Domain25 – 225201Glutamine amidotransferase type-1
Region256 – 520265Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00135
Region535 – 768234N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135

Sites

Active site1031For GATase activity By similarity
Active site1991For GATase activity By similarity
Active site2011For GATase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92411 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B2F215AA304B8B00

FASTA76883,655
        10         20         30         40         50         60 
MPSSTLIDHS PRNPNPSPPR ITASNVILID NYDSFTWNVY QYLVFEGAFV TVYRNDEITL 

        70         80         90        100        110        120 
DELIAKKPTQ LVISQVPDTR KEDVALAIEP LRTSVAKSPF SACAWESCIF YSYGGTVDVT 

       130        140        150        160        170        180 
GQILHGKTCP LKHDGKGVFA GVPQDVPVTR YHSLAGTHGT LPDCLEISAT IPANADAEIK 

       190        200        210        220        230        240 
EVIMGVRHKE YVIEGVQFHP ESILTEHGRL MMRNFLKMQG GTWAENERLQ KEAHAQAIGA 

       250        260        270        280        290        300 
AFSESAMVQR TDSRTHLQKI YDHRRAAVAE QKKIPSNRPV DLQAAYDSNL APPQINFPER 

       310        320        330        340        350        360 
LRQSPFKLSL MSEIKRASPS KGIISLSTCA PAQARLYAKA GARPISVLTE PEWFKGSIED 

       370        380        390        400        410        420 
LRAVRQSIEG MANRPALLRK EFIFDEYQIL EGRLAGADTV LVIVKMLETE LLERLLGLSD 

       430        440        450        460        470        480 
SVGMEPLVEV QNTDEMKIAV KLGAQVIGVN NRNLVNFEVD IGTTNRLIQM VPKETILCAL 

       490        500        510        520        530        540 
SGIAGPKDVE AYIKDGVGAV LVGEALMRAS DMSQFISELL GGPYKEVRAS SSSPIVKISG 

       550        560        570        580        590        600 
TRSEAAVAAV EAGADLIGII LAPGLKRTVT AETALSISEA VHKTKKPNVS KSGLLADSKT 

       610        620        630        640        650        660 
ASDFFDHGAS RLLETISRAL LVGVFRNQSL EYVLEQQRLL NLDVVQLHGQ EPIEWAKLVP 

       670        680        690        700        710        720 
VPVLKAFNPQ DHGIGTRGYH ALPLLDAGSG GSGKQLGLSD VKAAFTKDDG IKIILGRGLE 

       730        740        750        760 
PDNVQTTLAG LDEYRDRVYA VDVSSGVEED GQQSLDKIRS FVKAAKSL 

« Hide

References

[1]"Complementation of Cochliobolus heterostrophus trp-mutants produced by gene replacement."
Mullin P.G., Turgeon B.G., Yoder O.C.
Fungal Genet. Newsl. 40:51-53(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 48330 / C3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70035 Genomic DNA. Translation: CAA49629.1.

3D structure databases

ProteinModelPortalQ92411.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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

Family and domain databases

Gene3D3.20.20.70. 3 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_COCHE
AccessionPrimary (citable) accession number: Q92411
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 11, 2014
This is version 90 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