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P06531 (TRPG_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. 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
ORF Names:AN0648
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length768 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Induction

By tryptophan starvation. HAMAP-Rule MF_00135

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence caution

The sequence CBF89063.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence EAA65153.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 768768Multifunctional tryptophan biosynthesis protein HAMAP-Rule MF_00135
PRO_0000056859

Regions

Domain25 – 225201Glutamine amidotransferase type-1
Region252 – 516265Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00135
Region532 – 768237N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135

Sites

Active site1041For GATase activity By similarity
Active site1991For GATase activity By similarity
Active site2011For GATase activity By similarity

Experimental info

Sequence conflict1111I → H in CAA26232. Ref.2
Sequence conflict2491K → Q in CAA26232. Ref.2
Sequence conflict396 – 3983VLL → SYV in CAA26232. Ref.2
Sequence conflict396 – 3983VLL → SYV Ref.5
Sequence conflict410 – 4156RLYLYS → QTLSLF in CAA26232. Ref.2
Sequence conflict4101R → Q Ref.5
Sequence conflict473 – 48210VCALSGISGP → RLCTMRYFWT in CAA26232. Ref.2
Sequence conflict6811L → V in CAA26232. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06531 [UniParc].

Last modified October 19, 2011. Version 3.
Checksum: FEFE1374DF86151D

FASTA76883,127
        10         20         30         40         50         60 
MADTALVDHS PHHPTKAPRL ETASNVILID NYDSFTWNVY QYLVLEGATV TVIRNDEISL 

        70         80         90        100        110        120 
EELIAKKPTQ LVVSPGPGHP KSDAGISNAA IQYFAGKIPI FGVCMGQQCI IHSFGGKVDV 

       130        140        150        160        170        180 
TGEILHGKTS VLKHDGRGAY EGLPPSVIIT RYHSLAGTHS TIPECLEVSS FAQLGEDADK 

       190        200        210        220        230        240 
TVIMGVRHKQ FAVEGVQFHP ESILTEHGQT MFRNFLKLTA GTWEGNGKDV AQGGNFTAAA 

       250        260        270        280        290        300 
PNPPKATKKV SILEKIYDHR RAAVAKQKTI PSQRPSDLQA AYELSVAPPQ ISFPDRLRQS 

       310        320        330        340        350        360 
AYPLSLMAEI KRASPSKGLI AEHACAPAQA RQYAKAGASV ISVLTEPEWF KGSIDDLRAV 

       370        380        390        400        410        420 
RASLEGLTNR PAILRKEFIF DEYQILEARL AGADTVLLIV KMLDTELLTR LYLYSQSLGM 

       430        440        450        460        470        480 
EPLVEVNTPD EMKIAVDLGA QVIGVNNRDL TSFEVDLGTT SRLMDQVPES TIVCALSGIS 

       490        500        510        520        530        540 
GPKDVEAYKK DGVKAILVGE ALMRAPDTAA FVAELLGGQS KKLPLQSRNS PLVKICGTRT 

       550        560        570        580        590        600 
EEGARAAIEA GADLIGIILV EGRKRTVPDD VALQISKVVK STPRPTPYPT EVPQGDTDAT 

       610        620        630        640        650        660 
SVDYFDHSAT TLRHPTRALL VGVFLNQPLS YVLAQQQKLG LDVVQLHGSE PLEWSRLIPV 

       670        680        690        700        710        720 
PVIRKFGLDE FGIARRAYHT LPLLDSGAGG SGELLDQMRV KQILKSDDGL RVILAGGLDP 

       730        740        750        760 
LNVTEIIKQL DESGYKIVGV DVSSGVETNG VQDLDKIRSF VQAAKSAF 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Aspergillus niger trpC gene: structural relationship with analogous genes of other organisms."
Kos T., Kuijvenhoven A., Hessing H.G.M., Pouwels P.H., van den Hondel C.A.M.J.J.
Curr. Genet. 13:137-144(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primary structure of the trpC gene from Aspergillus nidulans."
Mullaney E.J., Hamer J.E., Roberti K.A., Yelton M.M., Timberlake W.E.
Mol. Gen. Genet. 199:37-45(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 7-768.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[5]"Developmental regulation of the Aspergillus nidulans trpC gene."
Yelton M.M., Hamer J.E., de Souza E.R., Mullaney E.J., Timberlake W.E.
Proc. Natl. Acad. Sci. U.S.A. 80:7576-7580(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-410.
[6]Genser K.F.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 719-768.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02390 Genomic DNA. Translation: CAA26232.1.
AACD01000009 Genomic DNA. Translation: EAA65153.1. Sequence problems.
U24705 Genomic DNA. Translation: AAB60292.1.
BN001308 Genomic DNA. Translation: CBF89063.1. Different initiation.
PIRS04518.
S07305.
RefSeqXP_658252.1. XM_653160.1.

3D structure databases

ProteinModelPortalP06531.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00002028; CADANIAP00002028; CADANIAG00002028.
GeneID2876427.
KEGGani:AN0648.2.

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280459.
OrthoDBEOG78WM1Q.

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_EMENI
AccessionPrimary (citable) accession number: P06531
Secondary accession number(s): C8VS06, Q5BFN2, Q92224
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 125 of the entry and version 3 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