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Q92370 (TRPG_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names:SPBC1539.09c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length759 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_00134_B

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00134_B

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. HAMAP-Rule MF_00134_B

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5. HAMAP-Rule MF_00134_B

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 – 759759Multifunctional tryptophan biosynthesis protein HAMAP-Rule MF_00134_B
PRO_0000056865

Regions

Domain27 – 223197Glutamine amidotransferase type-1
Region257 – 519263Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region536 – 759224N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Sites

Active site1081For GATase activity By similarity
Active site1971For GATase activity By similarity
Active site1991For GATase activity By similarity

Experimental info

Sequence conflict3871Q → E in CAA70348. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q92370 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 519E2EA55CB9B212

FASTA75983,040
        10         20         30         40         50         60 
MSEKVDVGES VKGDASENAV KEVAERPIVM IDNYDSFTWN VVQYLSNLEK RYPIMVFRND 

        70         80         90        100        110        120 
EITVDELEKL NPLKLVLSPG PGHPARDGGI CNEAISRFAG KIPILGVCMG LQCIFETMGG 

       130        140        150        160        170        180 
KVDSAGEIIH GKVSKINHDG LGFYQGIPQN ISVTRYHSLA GKISSLPDCL DVTSWTENGV 

       190        200        210        220        230        240 
IMGARHKKYA IEGVQYHPES ILSEYGKEYI QNFLNLTAGT WEENGIVMPT KNNAFNAAMR 

       250        260        270        280        290        300 
ENSNSVSSTK IRKQESILEK IHAQRLIDIA ESKRKPGLSV GDLQTYLNLN IAPPCINFYE 

       310        320        330        340        350        360 
RLKQSKPALM AEVKRASPSK GDIKLDANAA IQALTYAQVG ASVISVLTEP KWFKGSLNDL 

       370        380        390        400        410        420 
FVARKAVEHV ANRPAILRKD FIIDPYQIME ARLNGADSVL LIVAMLSREQ LESLYKFSKS 

       430        440        450        460        470        480 
LGMEPLVEVN CAEEMKTAIE LGAKVIGVNN RNLHSFEVDL STTSKLAEMV PDDVILAALS 

       490        500        510        520        530        540 
GISSPADVAH YSSQGVSAVL VGESLMRASD PAAFARELLN LSSSEISNGK KTSTPLVKVC 

       550        560        570        580        590        600 
GTRSLLAAKT IVESGGDLIG LIFVEKSKRK VDLSVAKEIS HFVHTTNRKH ISPKKAVTGQ 

       610        620        630        640        650        660 
SWFDHQYENL ASSPHPLLVG VFQNQPLEYI RSIIAEVNLD IVQLHGQEPF EWIHMLDRPV 

       670        680        690        700        710        720 
IKVFPLNSSE ISRPNYHIVP LIDAYVGGES GGLGKKVDWE AASFIPVSYV LAGGLTPKNV 

       730        740        750 
QDAISVSRPA VVDVSSGVET DGKQDLEKIK AFINAVKEL 

« Hide

References

« Hide 'large scale' references
[1]David C., Couzin N., Lauquin G.J.-M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09137 mRNA. Translation: CAA70348.1.
CU329671 Genomic DNA. Translation: CAB51341.1.
PIRT39468.
T46566.
RefSeqNP_596823.1. NM_001023843.1.

3D structure databases

ProteinModelPortalQ92370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276517. 3 interactions.
MINTMINT-4701389.
STRING4896.SPBC1539.09c-1.

Protein family/group databases

MEROPSC26.A25.

Proteomic databases

MaxQBQ92370.
PaxDbQ92370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1539.09c.1; SPBC1539.09c.1:pep; SPBC1539.09c.
GeneID2539973.
KEGGspo:SPBC1539.09c.

Organism-specific databases

PomBaseSPBC1539.09c.

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280459.
KOK13501.
OMAPVLGVCM.
OrthoDBEOG78WM1Q.
PhylomeDBQ92370.

Enzyme and pathway databases

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

Family and domain databases

Gene3D3.20.20.70. 2 hits.
3.40.50.880. 1 hit.
HAMAPMF_00134_B. IGPS_B.
MF_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...

Other

NextBio20801116.

Entry information

Entry nameTRPG_SCHPO
AccessionPrimary (citable) accession number: Q92370
Secondary accession number(s): Q9UUF5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 114 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways