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P24773 (TRPG_PENCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. 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
OrganismPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifier5076 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum 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_0000056862

Regions

Domain23 – 223201Glutamine amidotransferase type-1
Region239 – 503265Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00135
Region519 – 752234N-(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
P24773 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: D6256C3818E22FDB

FASTA75281,035
        10         20         30         40         50         60 
MADLVDHSPH HATKAAKLAS ASNVILIDNY DSFTWNIYQY LVLEGATVTV YRNDEVTVED 

        70         80         90        100        110        120 
LVAKKPTQLV ISPGPGHPDT DAGISNAVIK HFSGKVPIFG VCMGQQCMIT SFGGKVDVTG 

       130        140        150        160        170        180 
EILHGKTSEL KHDSKGVYQG LPTSLEVTRY HSLAGTHSTI PDCLEVTSRV ELGDASGKNI 

       190        200        210        220        230        240 
IMGVRHKEFA VEGVQFHPES ILTQYGRKMF RNFLELTAGT WDNKQGAAVA APADKKLSIL 

       250        260        270        280        290        300 
DKIYAHRKNA VDEQKKIPAL RPEALQAAYD LNIAPPQLSF PDRLRQSDYP LSLMAEIKRA 

       310        320        330        340        350        360 
SPSKGIISAN VCAPAQAREY AKAGASVISV LTEPEWFKGT IDDLRAVRQS LEGLPNRPAV 

       370        380        390        400        410        420 
LRKEFVFEEY QILEARLAGA DTVLLIVKML DIELLTRLYH YSRSLGMEPL VEVNTPEEMK 

       430        440        450        460        470        480 
IAVDLGSEVI GVNNRDLTSF EVDLGTTSRL MDQVPESTIV CALSGISGPQ DVEAYKKEGV 

       490        500        510        520        530        540 
KAILVGEALM RAPDTSAFVA QLLGGSNQNF AGASPSSPLV KICGTRTEEG ALAAIQAGAD 

       550        560        570        580        590        600 
LIGIIMVQGR SRLVPDDVAL GISRVVKSTP RPADTLQQPS SATSLEWFDH STNILRHPSR 

       610        620        630        640        650        660 
ALLVGVFMNQ PLSYVVSQQQ KLGLDVVQLH GSEPLEWSSL IPVPVIRKFA PGDIGIARRA 

       670        680        690        700        710        720 
YHTLPLLDSG AGGSGELLEE SGVKKVLDSD EGLRVILAGG LNPDNVAGTV KKLGQSGQKV 

       730        740        750 
VGLDVSSGVE TNGAQDLEKI RAFVKSAKSI RQ 

« Hide

References

[1]"The complete nucleotide sequence of the trpC gene from Penicillium chrysogenum."
Penalva M.A., Sanchez F.
Nucleic Acids Res. 15:1874-1874(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05033 Genomic DNA. Translation: CAA28707.1.
PIRS30084.

3D structure databases

ProteinModelPortalP24773.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

PhylomeDBP24773.

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_PENCH
AccessionPrimary (citable) accession number: P24773
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 11, 2014
This is version 98 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