P27710 (TRPG_CRYNH) Reviewed, UniProtKB/Swiss-Prot

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:

1. Glutamine amidotransferase
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:	CNAG_04501

Organism

Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) [Complete proteome]

Taxonomic identifier

235443 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex › Cryptococcus neoformans › Cryptococcus neoformans var. grubii

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

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
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_0000056858
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
Experimental info
	Sequence conflict	295 – 309	15	KGDIA…PQQAL → FQGRNAPTLLLLRST Ref.2
	Sequence conflict	504	1	P → S in AAA51445. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P27710 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: FE31FEF7BFC5FC91	FASTA	752	80,194
	10 20 30 40 50 60 MGFTLLIDNY DSFTWNIYAD LASVGGNPFV VRNDKITLKE IEGMFADGEL ERIVISPGPG 70 80 90 100 110 120 HPRTDSGVSR DVIAWGMGKL PILGVCMGLE CIVDLLGGEI AYAGEIKHGK TSLVQHDSIG 130 140 150 160 170 180 VFHNLPQFLS STRYHSLSAQ IQSLPSVLQV TSTTKESGVI MGVRHRTFTV EAVQYHPESC 190 200 210 220 230 240 MSEGGRGLMA NFIQMKGGKW GGENAWCGVP AEGEGEQPKA KTNGAPSLPT ILNKIHAQRL 250 260 270 280 290 300 LDVEQAEKIP ATTPANVSTS LSLYTSPPLI NFRGRMVSTP HTAVMAEIKR ASPSKGDIAP 310 320 330 340 350 360 TASAPQQALK 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 EVVPKPRPLV KICGIRSTND AKLAINAGAD LLGVILVPGT 550 560 570 580 590 600 KRCISTSTAR EISALVQSAR SQSSSKPLEP SLSSPWFTSQ SALLSSRRKP LLVGVFQNQS 610 620 630 640 650 660 LSDILSAVDE IGLDLVQLHG DEPQAWAKFI PVPVVKVFRV SPEGIVRGGE IRRPGLNQAI 670 680 690 700 710 720 LLDAGGASGG GGEGKAFPWE HAKRLIQSGE VGSEGHVPLP VILAGGLTPE NVGQAIEQAG 730 740 750 EGVWCVDVSS GVEGEGGKVK EKVEAFVKAV RG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Cryptococcus neoformans grubii H99." The Broad Institute Genome Sequencing Platform Birren B., Cuomo C., Gargeya S., Jaffe D., Young S.K., Wortman J., Zeng Q., Alvarado L., Dietrich F., Allen A., Stajich J.E., Heitman J., Kronstad J. Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003828 Genomic DNA. Translation: AFR97220.1. M74901 Genomic DNA. Translation: AAA51445.1. Sequence problems.
PIR	JN0451.
3D structure databases
ProteinModelPortal	P27710.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_CRYNH

Accession

Primary (citable) accession number: P27710
Secondary accession number(s): J9VZN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	June 21, 2005
Last modified:	April 3, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program