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Protein

Multifunctional tryptophan biosynthesis protein

Gene

trp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.

Catalytic activityi

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.
Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1, 3 and 4 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Multifunctional tryptophan biosynthesis protein (trp1), Probable anthranilate synthase component 1 (trp3)
  2. Anthranilate phosphoribosyltransferase (trp4)
  3. Multifunctional tryptophan biosynthesis protein (trp1)
  4. Multifunctional tryptophan biosynthesis protein (trp1)
  5. Tryptophan synthase (trp2)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei108Nucleophile; for GATase activityBy similarity1
Binding sitei112GlutamineBy similarity1
Active sitei197For GATase activityBy similarity1
Active sitei199For GATase activityBy similarity1

GO - Molecular functioni

  • anthranilate synthase activity Source: PomBase
  • indole-3-glycerol-phosphate lyase activity Source: PomBase
  • indole-3-glycerol-phosphate synthase activity Source: UniProtKB-EC
  • phosphoribosylanthranilate isomerase activity Source: PomBase
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • glutamine metabolic process Source: UniProtKB-KW
  • tryptophan biosynthetic process Source: PomBase

Keywords - Molecular functioni

Decarboxylase, Isomerase, Lyase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00042.
UPA00035; UER00043.

Protein family/group databases

MEROPSiC26.A25.

Names & Taxonomyi

Protein namesi
Recommended name:
Multifunctional tryptophan biosynthesis protein
Including the following 3 domains:
Anthranilate synthase component 2 (EC:4.1.3.27)
Short name:
AS
Alternative name(s):
Anthranilate synthase, glutamine amidotransferase component
Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
Short name:
IGPS
N-(5'-phosphoribosyl)anthranilate isomerase (EC:5.3.1.24)
Short name:
PRAI
Gene namesi
Name:trp1
ORF Names:SPBC1539.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1539.09c.
PomBaseiSPBC1539.09c. trp1.

Subcellular locationi

GO - Cellular componenti

  • anthranilate synthase complex Source: PomBase
  • cytosol Source: PomBase

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000568651 – 759Multifunctional tryptophan biosynthesis proteinAdd BLAST759

Proteomic databases

MaxQBiQ92370.
PRIDEiQ92370.

Interactioni

Protein-protein interaction databases

BioGridi276517. 2 interactors.
MINTiMINT-4701389.

Structurei

3D structure databases

ProteinModelPortaliQ92370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 223Glutamine amidotransferase type-1Add BLAST197

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 82Glutamine bindingBy similarity3
Regioni158 – 159Glutamine bindingBy similarity2
Regioni257 – 519Indole-3-glycerol phosphate synthaseAdd BLAST263
Regioni536 – 759N-(5'-phosphoribosyl)anthranilate isomeraseAdd BLAST224

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000280459.
InParanoidiQ92370.
KOiK13501.
OMAiMPNRPAI.
OrthoDBiEOG092C1PKC.
PhylomeDBiQ92370.

Family and domain databases

CDDicd00331. IGPS. 1 hit.
cd00405. PRAI. 1 hit.
Gene3Di3.20.20.70. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00134_B. IGPS_B. 1 hit.
MF_00135. PRAI. 1 hit.
InterProiIPR013785. 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.
IPR011060. RibuloseP-bd_barrel.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
PIRSFiPIRSF001382. TrpG-trpC-trpF. 1 hit.
SUPFAMiSSF51366. SSF51366. 3 hits.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
PS00614. IGPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKVDVGES VKGDASENAV KEVAERPIVM IDNYDSFTWN VVQYLSNLEK
60 70 80 90 100
RYPIMVFRND EITVDELEKL NPLKLVLSPG PGHPARDGGI CNEAISRFAG
110 120 130 140 150
KIPILGVCMG LQCIFETMGG KVDSAGEIIH GKVSKINHDG LGFYQGIPQN
160 170 180 190 200
ISVTRYHSLA GKISSLPDCL DVTSWTENGV IMGARHKKYA IEGVQYHPES
210 220 230 240 250
ILSEYGKEYI QNFLNLTAGT WEENGIVMPT KNNAFNAAMR ENSNSVSSTK
260 270 280 290 300
IRKQESILEK IHAQRLIDIA ESKRKPGLSV GDLQTYLNLN IAPPCINFYE
310 320 330 340 350
RLKQSKPALM AEVKRASPSK GDIKLDANAA IQALTYAQVG ASVISVLTEP
360 370 380 390 400
KWFKGSLNDL FVARKAVEHV ANRPAILRKD FIIDPYQIME ARLNGADSVL
410 420 430 440 450
LIVAMLSREQ LESLYKFSKS LGMEPLVEVN CAEEMKTAIE LGAKVIGVNN
460 470 480 490 500
RNLHSFEVDL STTSKLAEMV PDDVILAALS GISSPADVAH YSSQGVSAVL
510 520 530 540 550
VGESLMRASD PAAFARELLN LSSSEISNGK KTSTPLVKVC GTRSLLAAKT
560 570 580 590 600
IVESGGDLIG LIFVEKSKRK VDLSVAKEIS HFVHTTNRKH ISPKKAVTGQ
610 620 630 640 650
SWFDHQYENL ASSPHPLLVG VFQNQPLEYI RSIIAEVNLD IVQLHGQEPF
660 670 680 690 700
EWIHMLDRPV IKVFPLNSSE ISRPNYHIVP LIDAYVGGES GGLGKKVDWE
710 720 730 740 750
AASFIPVSYV LAGGLTPKNV QDAISVSRPA VVDVSSGVET DGKQDLEKIK

AFINAVKEL
Length:759
Mass (Da):83,040
Last modified:April 27, 2001 - v2
Checksum:i519E2EA55CB9B212
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti387Q → E in CAA70348 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09137 mRNA. Translation: CAA70348.1.
CU329671 Genomic DNA. Translation: CAB51341.1.
PIRiT39468.
T46566.
RefSeqiNP_596823.1. NM_001023843.1.

Genome annotation databases

EnsemblFungiiSPBC1539.09c.1; SPBC1539.09c.1:pep; SPBC1539.09c.
GeneIDi2539973.
KEGGispo:SPBC1539.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09137 mRNA. Translation: CAA70348.1.
CU329671 Genomic DNA. Translation: CAB51341.1.
PIRiT39468.
T46566.
RefSeqiNP_596823.1. NM_001023843.1.

3D structure databases

ProteinModelPortaliQ92370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276517. 2 interactors.
MINTiMINT-4701389.

Protein family/group databases

MEROPSiC26.A25.

Proteomic databases

MaxQBiQ92370.
PRIDEiQ92370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1539.09c.1; SPBC1539.09c.1:pep; SPBC1539.09c.
GeneIDi2539973.
KEGGispo:SPBC1539.09c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1539.09c.
PomBaseiSPBC1539.09c. trp1.

Phylogenomic databases

HOGENOMiHOG000280459.
InParanoidiQ92370.
KOiK13501.
OMAiMPNRPAI.
OrthoDBiEOG092C1PKC.
PhylomeDBiQ92370.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00042.
UPA00035; UER00043.

Miscellaneous databases

PROiQ92370.

Family and domain databases

CDDicd00331. IGPS. 1 hit.
cd00405. PRAI. 1 hit.
Gene3Di3.20.20.70. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00134_B. IGPS_B. 1 hit.
MF_00135. PRAI. 1 hit.
InterProiIPR013785. 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.
IPR011060. RibuloseP-bd_barrel.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
PIRSFiPIRSF001382. TrpG-trpC-trpF. 1 hit.
SUPFAMiSSF51366. SSF51366. 3 hits.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
PS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRPG_SCHPO
AccessioniPrimary (citable) accession number: Q92370
Secondary accession number(s): Q9UUF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: November 30, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.