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P18483 (TRPG_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. 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:trpC
OrganismAspergillus awamori (Black koji mold)
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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_0000056854

Regions

Domain25 – 223199Glutamine amidotransferase type-1
Region253 – 517265Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00135
Region533 – 768236N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135

Sites

Active site1021For GATase activity By similarity
Active site1971For GATase activity By similarity
Active site1991For GATase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P18483 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: E3C0DB1AB10225CE

FASTA76882,657
        10         20         30         40         50         60 
MADSGLVDHS PHHPTKAAQL NTASNVILID NYDSFTWNVY LVLEGATVNV FRNDQITLEE 

        70         80         90        100        110        120 
LIAKKPTQLV ISPGPGHPET DAGISSAAIQ YFSGKIPIFG VCMGQQCIIT CFGGKVDVTG 

       130        140        150        160        170        180 
EILHGKTSAL KHDGKGAYEG LPDSLALTRY HSLAGTHATI PDCLEVSSSV QLTDDSNKDV 

       190        200        210        220        230        240 
IMGVRHKKLA VEGVQFHPES ILTEYGRTMF RNFLKLTAGT WEGNGKHFDE QSNTTKATVS 

       250        260        270        280        290        300 
SNTAPKTDKK LSILERIYDH RRAAVAVQKT IPSQRPADLQ AAYDLNLAPP QVPFPARLRQ 

       310        320        330        340        350        360 
SPYPLSLMAE IKRASPSKGM IAENACAPAQ ARQYAKAGAS VISVLTEPEW FKGSIDDLRA 

       370        380        390        400        410        420 
VRQSLEGLTN RPAILRKEFV FDEYQILEAR LAGADTVLLI VKMLSVELLT RLYHYSRSLG 

       430        440        450        460        470        480 
MEPLVEVNTP EEMKIAVDLG AEVIGVNNRD LTSFEVDLGT TSRLMDQVPS STIVCALSGI 

       490        500        510        520        530        540 
SGPKDVEAYK KEGVKAILVG EALMRAADTA AFIAELLGGS SQNVSKESRS SPLVKICGTR 

       550        560        570        580        590        600 
SEEAARAAIE AGADLIGIIM VQGRTRCVPD DVALRISQVV KSIPKPAGQT PPTSRGTPAA 

       610        620        630        640        650        660 
ASVEYFDHSA RILRHPSRAL LVGVFQNQPL DYILSQQQKL GLDVVQLHGS EPLEWAKLIP 

       670        680        690        700        710        720 
VPVIRKFGLD EPAIARRAYH SLPLLDSGVG GTGELLDQSR VQNVLDKDSG LRVILAGGLD 

       730        740        750        760 
PTNVAGIVQK LGESGRKVVG VDVSSGVESD GAQDLGKIRA FVQAVRGL 

« Hide

References

[1]"Complete genomic sequence encoding trpC from Aspergillus niger var. awamori."
Adams R.R., Royer T.
Nucleic Acids Res. 18:4931-4931(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 22342 / NRRL 3112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53576 Genomic DNA. Translation: CAA37640.1.
PIRS11161.

3D structure databases

ProteinModelPortalP18483.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP18483.

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.
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]
PANTHERPTHR11922:SF3. PTHR11922:SF3. 1 hit.
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_ASPAW
AccessionPrimary (citable) accession number: P18483
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 19, 2014
This is version 102 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