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P00908 (TRPG_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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:trp-1
Synonyms:trpg-trpc-trpf, tryp-1
ORF Names:NCU00200
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length762 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

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. HAMAP-Rule MF_00135

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

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.

Subunit structure

Tetramer of two components I and two components II.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 762762Multifunctional tryptophan biosynthesis protein HAMAP-Rule MF_00135
PRO_0000056861

Regions

Domain25 – 224200Glutamine amidotransferase type-1
Region251 – 515265Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00135
Region531 – 762232N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00135

Sites

Active site1041For GATase activity By similarity
Active site1981For GATase activity By similarity
Active site2001For GATase activity By similarity

Experimental info

Sequence conflict3371A → G Ref.1
Sequence conflict5111I → V Ref.1
Sequence conflict5231P → S Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00908 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: C058B21FF4B7C5BB

FASTA76282,559
        10         20         30         40         50         60 
MSSSSVVDHS PHDSAPSPLV PTASNLILID NYDSFTWNVY QYLVLEGAKV TVFRNDQITI 

        70         80         90        100        110        120 
DELIAKNPTQ LVISPGPGHP GTDSGISRDA IRHFAGKIPI FGVCMGQQCI FDVYGGDVCF 

       130        140        150        160        170        180 
AGEILHGKTS PLRHDGKGAY AGLSQDLPVT RYHSLAGTHV TLPECLEVTS WIAKEDGSKG 

       190        200        210        220        230        240 
VIMGVRHKEY TIEGVQFHPE SILSAEGRGM FRNFLHMQGG TWAENERLQK AAQAQAANTK 

       250        260        270        280        290        300 
SDAPTPKKSN ILQKIYAHRK AAVDAQKQIP SLRPSDLQAA YNLSIAPPQI SLVDRLRNSP 

       310        320        330        340        350        360 
FDVALCAEIK RASPSKGVFA LDIDAPSQAR KYALAGASVI SVLTEPEWFK GSIDDLRAVR 

       370        380        390        400        410        420 
QVLNGMPNRP AVLRKEFIFD EYQILEARLA GADTVLLIVK MLEYELLERL YKYSLSLGME 

       430        440        450        460        470        480 
PLVEVQNTEE MATAIKLGAK VIGVNNRNLE SFEVDLGTTG RLRSMVPSDT FLCALSGINT 

       490        500        510        520        530        540 
HQDVLDCKRD GVNGILVGEA IMRAPDATQF IRELCAGLTG PVPKSAAEPL LVKICGTRSA 

       550        560        570        580        590        600 
EAAAEAIKAG ADLVGMIMVP GTKRCVDHET ALSISQAVHM SKKTGSTEVS SQASKSARDF 

       610        620        630        640        650        660 
FNINAEIIRK RGPLLVGVFM NQPLEEVLEK QHLYDLDIVQ LHGDEPLEWA NLIPVPVVRK 

       670        680        690        700        710        720 
FKPGQVGLAT RGYHAVPLLD SGAGSGTLLD LESVKKELEK DEQVTVLLAG GLEPSNVVET 

       730        740        750        760 
VKSLGPLSER VIGVDVSSGV EEGGKQSLEK IREFVKAAKS VR 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the trifunctional trp-1 gene from Neurospora crassa and its aberrant expression in Escherichia coli."
Schechtman M.G., Yanofsky C.
J. Mol. Appl. Genet. 2:83-99(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01252 Genomic DNA. No translation available.
CM002238 Genomic DNA. Translation: ESA43300.1.
CM002238 Genomic DNA. Translation: ESA43301.1.
PIRNNNC2. A01130.
RefSeqXP_956585.1. XM_951492.1.

3D structure databases

ProteinModelPortalP00908.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU00200.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000000483; EFNCRP00000000483; EFNCRG00000000483.
GeneID3872732.
KEGGncr:NCU00200.

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280459.
KOK13501.
OrthoDBEOG78WM1Q.

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_NEUCR
AccessionPrimary (citable) accession number: P00908
Secondary accession number(s): Q7RV57, U9W354
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 128 of the entry and version 2 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