Anthranilate synthase component 2 - Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Anthranilate synthase component 2
EC=4.1.3.27

Alternative name(s):
Anthranilate synthase component II

Including the following 3 domains:

Glutamine amidotransferase
Indole-3-glycerol phosphate synthase
Short name=IGPS
EC=4.1.1.48
N-(5'-phosphoribosyl)anthranilate isomerase
Short name=PRAI
EC=5.3.1.24

Gene names

Name:	TRP1
Ordered Locus Names:	CNI00560

Organism

Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) [Reference proteome]

Taxonomic identifier

214684 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex ›

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Protein existence	Predicted

General annotation (Comments)

Function	Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
Catalytic activity	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	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5. 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Domain	Glutamine amidotransferase
Molecular function	Decarboxylase Isomerase Lyase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	anthranilate synthase activity Inferred from electronic annotation. Source: EC indole-3-glycerol-phosphate synthase activity Inferred from electronic annotation. Source: EC phosphoribosylanthranilate isomerase activity Inferred from electronic annotation. Source: EC transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 752

752

Anthranilate synthase component 2

PRO_0000056857

Regions

Domain

3 – 202

200

Glutamine amidotransferase type-1

Region

231 – 495

265

Indole-3-glycerol phosphate synthase

Region

509 – 752

244

N-(5'-phosphoribosyl)anthranilate isomerase

Sites

Active site

86

1

For GATase activity By similarity

Active site

176

1

For GATase activity By similarity

Active site

178

1

For GATase activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0CN86 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: BE85651BED85BBE5
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FASTA

752

80,473

        10         20         30         40         50         60 
MGFTLLIDNY DSFTWNIYAD LASVGGNPYV VRNDKITLKE IEGMFSDGEL ERIVISPGPG 

        70         80         90        100        110        120 
HPRTDSGVSR DVIAWGMGKL PILGVCMGLE CIVDLLGGEI AYAGEIKHGK TSLVQHDSIG 

       130        140        150        160        170        180 
VFHNLPQFLS STRYHSLSAQ IQSLPSVLQV TSTTKESGVI MGVRHRTYTV EAVQYHPESC 

       190        200        210        220        230        240 
MSEGGRGLMA NFIQMKGGKW GGENAWCGVP AEGEEEQPKA KTNGAPSLPT ILNRIHAQRL 

       250        260        270        280        290        300 
LDVEQAEKVP ATSPANVSTS LSLYASPPLI NFRDRMVSTP HTAVMAEIKR ASPSKGDIAP 

       310        320        330        340        350        360 
TASAPEQALK YALAGASVIS VLTEPTWFKG SLLDMLAVRN AVDSLPNRPA ILRKDFVLSK 

       370        380        390        400        410        420 
YMIDEARLYG ADTVLLIVAM LEPQQLKELY DYSVSLGMEP LVEVNNPTEL SLALEIGSKV 

       430        440        450        460        470        480 
IGVNNRNLHD FNVDMSTTSR VNAALNGRDV VLCALSGISS HEDVEKYVKE GVKGVLVGEA 

       490        500        510        520        530        540 
LMRASDTKAF LRSLIGLPPL EVVPKSRPLV KICGIRSTDD AKLAISAGAD LLGVILVPGT 

       550        560        570        580        590        600 
KRCISTSTAR EISALVQSAR SQSSSKPLEP SLSSPWFTTQ SDLLSSRRKP LLVGVFQNQS 

       610        620        630        640        650        660 
LSDILSAVEE IGLDLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE FRRPGLNQAI 

       670        680        690        700        710        720 
LLDAGGVSGG GGEGKAFPWE HAKRLIQSGE VGSEGHMPLP VILAGGLTPE NVGQAIEQAG 

       730        740        750 
EGVWCVDVSS GVEGEGGKVK EKVEAFVKAV RG

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References

[1]

"The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.

Hyman R.W.
Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JEC21 / ATCC MYA-565.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017349 Genomic DNA. Translation: AAW45488.1.
RefSeq	XP_572795.1. XM_572795.1.
UniGene	Fne.446.
3D structure databases
ProteinModelPortal	P0CN86.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3259660.
KEGG	cne:CNI00560.
Phylogenomic databases
KO	K13501.
Enzyme and pathway databases
UniPathway	UPA00035; UER00040. UPA00035; UER00042. UPA00035; UER00043.
Family and domain databases
Gene3D	3.20.20.70. 2 hits.
InterPro	IPR013785. Aldolase_TIM. IPR016302. Anthranilate_synth_II. IPR017926. GATASE_1. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GlycerolPSynthase_CS. IPR001240. PRAI. IPR011060. RibuloseP-bd_barrel. IPR006221. TrpG/PapA. [Graphical view]
PANTHER	PTHR11922:SF3. PTHR11922:SF3. 1 hit.
Pfam	PF00117. GATase. 1 hit. PF00218. IGPS. 1 hit. PF00697. PRAI. 1 hit. [Graphical view]
PIRSF	PIRSF001382. TrpG-trpC-trpF. 1 hit.
SUPFAM	SSF51366. RibP_bind_barrel. 2 hits.
TIGRFAMs	TIGR00566. trpG_papA. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. PS00614. IGPS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRPG_CRYNJ

Accession

Primary (citable) accession number: P0CN86
Secondary accession number(s): Q55NN6, Q5KC22

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 28, 2011
Last sequence update:	June 28, 2011
Last modified:	March 6, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents