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Protein

Multifunctional tryptophan biosynthesis protein

Gene

TRP1

Organism
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.

Pathway:iL-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)
  2. no protein annotated in this organism
  3. Multifunctional tryptophan biosynthesis protein (TRP1)
  4. Multifunctional tryptophan biosynthesis protein (TRP1)
  5. no protein annotated in this organism
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861For GATase activityBy similarity
Active sitei176 – 1761For GATase activityBy similarity
Active sitei178 – 1781For GATase activityBy similarity

GO - Molecular functioni

GO - Biological processi

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.

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:CNAG_04501
OrganismiCryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Taxonomic identifieri235443 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
ProteomesiUP000010091 Componenti: Chromosome 9

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 752752Multifunctional tryptophan biosynthesis proteinPRO_0000056858Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP27710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 202200Glutamine amidotransferase type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 495265Indole-3-glycerol phosphate synthaseAdd
BLAST
Regioni509 – 752244N-(5'-phosphoribosyl)anthranilate isomeraseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

OrthoDBiEOG78WM1Q.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00135. PRAI.
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.

P27710-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFTLLIDNY DSFTWNIYAD LASVGGNPFV VRNDKITLKE IEGMFADGEL
60 70 80 90 100
ERIVISPGPG HPRTDSGVSR DVIAWGMGKL PILGVCMGLE CIVDLLGGEI
110 120 130 140 150
AYAGEIKHGK TSLVQHDSIG VFHNLPQFLS STRYHSLSAQ IQSLPSVLQV
160 170 180 190 200
TSTTKESGVI MGVRHRTFTV EAVQYHPESC MSEGGRGLMA NFIQMKGGKW
210 220 230 240 250
GGENAWCGVP AEGEGEQPKA KTNGAPSLPT ILNKIHAQRL LDVEQAEKIP
260 270 280 290 300
ATTPANVSTS LSLYTSPPLI NFRGRMVSTP HTAVMAEIKR ASPSKGDIAP
310 320 330 340 350
TASAPQQALK YALAGASVIS VLTEPTWFKG SLLDMLAVRN AVDSLPNRPA
360 370 380 390 400
ILRKDFVLSK YMIDEARLYG ADTVLLIVAM LEPQQLKELY DYSVSLGMEP
410 420 430 440 450
LVEVNNPTEL SLALEIGSKV IGVNNRNLHD FNVDMSTTSR VNAALNGRDV
460 470 480 490 500
VLCALSGISS HEDVEKYVKE GVKGVLVGEA LMRASDTKAF LRSLIGLPPL
510 520 530 540 550
EVVPKPRPLV KICGIRSTND AKLAINAGAD LLGVILVPGT KRCISTSTAR
560 570 580 590 600
EISALVQSAR SQSSSKPLEP SLSSPWFTSQ SALLSSRRKP LLVGVFQNQS
610 620 630 640 650
LSDILSAVDE IGLDLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE
660 670 680 690 700
IRRPGLNQAI LLDAGGASGG GGEGKAFPWE HAKRLIQSGE VGSEGHVPLP
710 720 730 740 750
VILAGGLTPE NVGQAIEQAG EGVWCVDVSS GVEGEGGKVK EKVEAFVKAV

RG
Length:752
Mass (Da):80,194
Last modified:June 21, 2005 - v2
Checksum:iFE31FEF7BFC5FC91
GO

Sequence cautioni

The sequence AAA51445.1 differs from that shown. Reason: Frameshift at positions 297, 302, 307, 310 and 716. Curated
The sequence AAA51445.1 differs from that shown. Reason: Erroneous termination at position 324. Translated as Glu.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 30915KGDIA…PQQAL → FQGRNAPTLLLLRST (PubMed:1452032).CuratedAdd
BLAST
Sequence conflicti504 – 5041P → S in AAA51445 (PubMed:1452032).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003828 Genomic DNA. Translation: AFR97220.1.
M74901 Genomic DNA. Translation: AAA51445.1. Sequence problems.
PIRiJN0451.
RefSeqiXP_012051839.1. XM_012196449.1.

Genome annotation databases

GeneIDi23887910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003828 Genomic DNA. Translation: AFR97220.1.
M74901 Genomic DNA. Translation: AAA51445.1. Sequence problems.
PIRiJN0451.
RefSeqiXP_012051839.1. XM_012196449.1.

3D structure databases

ProteinModelPortaliP27710.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23887910.

Phylogenomic databases

OrthoDBiEOG78WM1Q.

Enzyme and pathway databases

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

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00135. PRAI.
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...

Publicationsi

  1. "Analysis of the genome and transcriptome of Cryptococcus neoformans var. grubii reveals complex RNA expression and microevolution leading to virulence attenuation."
    Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V., Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F., Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A., Gaillardin C., Gerik K.J.
    , Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A., Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A., Cuomo C.A., Dietrich F.S.
    PLoS Genet. 10:E1004261-E1004261(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: H99 / ATCC 208821 / CBS 10515 / FGSC 9487.
  2. "Cloning the Cryptococcus neoformans TRP1 gene by complementation in Saccharomyces cerevisiae."
    Perfect J.R., Rude T.H., Penning L.M., Johnston S.A.
    Gene 122:213-217(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-752.

Entry informationi

Entry nameiTRPG_CRYNH
AccessioniPrimary (citable) accession number: P27710
Secondary accession number(s): J9VZN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 21, 2005
Last modified: July 22, 2015
This is version 93 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.