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Protein

Multifunctional tryptophan biosynthesis protein

Gene

trp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -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

GO - Biological processi

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

Keywordsi

Molecular functionDecarboxylase, Isomerase, Lyase, Multifunctional enzyme
Biological processAmino-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ92370
PaxDbiQ92370
PRIDEiQ92370

PTM databases

iPTMnetiQ92370

Interactioni

Protein-protein interaction databases

BioGridi276517, 2 interactors
STRINGi4896.SPBC1539.09c.1

Structurei

3D structure databases

ProteinModelPortaliQ92370
SMRiQ92370
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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000280459
InParanoidiQ92370
KOiK13501
OMAiWFKGSIE
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
InterProiView protein in InterPro
IPR013785 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
PfamiView protein in Pfam
PF00117 GATase, 1 hit
PF00218 IGPS, 1 hit
PF00697 PRAI, 1 hit
PIRSFiPIRSF001382 TrpG-trpC-trpF, 1 hit
SUPFAMiSSF51366 SSF51366, 3 hits
SSF52317 SSF52317, 1 hit
TIGRFAMsiTIGR00566 trpG_papA, 1 hit
PROSITEiView protein in PROSITE
PS51273 GATASE_TYPE_1, 1 hit
PS00614 IGPS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiTRPG_SCHPO
AccessioniPrimary (citable) accession number: Q92370
Secondary accession number(s): Q9UUF5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: April 25, 2018
This is version 140 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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