P25170 (TRPG_PHACH) 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:

TRPC

Organism

Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)

Taxonomic identifier

5306 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetes incertae sedis › Corticiales › Corticiaceae › Phanerochaete

Protein attributes

Sequence length	788 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	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 – 788	788	Anthranilate synthase component 2		PRO_0000056863
Regions
	Domain	12 – 207	196	Glutamine amidotransferase type-1
	Region	238 – 503	266	Indole-3-glycerol phosphate synthase
	Region	520 – 788	269	N-(5'-phosphoribosyl)anthranilate isomerase
Sites
	Active site	91	1	For GATase activity By similarity
	Active site	181	1	For GATase activity By similarity
	Active site	183	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25170 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 20108D088803D787	FASTA	788	85,345
	10 20 30 40 50 60 MSLPPHLCVP IDILMIDNFD SFTWNLYQSL CLLGADVTVI RNDAIPRSAI PQLRIKRLIV 70 80 90 100 110 120 SPGPGHPQTD SGISREAIKY FAGKVPIMGV CMGLECVVDV FGGQIAYAGE IMHGKVSGIR 130 140 150 160 170 180 HDARGCFKDL PQGIQSTRYH SLSAGVKTLP DELAVTAVTE HERVIMGIRH RKYTVEAVQY 190 200 210 220 230 240 HPESILSESG DDLLRHFMKL KGGTWEENPE FRVLDPSLPA FEIGSQPAAS TSAKIPTILE 250 260 270 280 290 300 KICAQRQKDV DQAKATPGTT PEDLKTLLSM KLSPPQISFP DRLKAAEVKP ALMAEVKRAS 310 320 330 340 350 360 PSKGPIAMNG NAAQQALTYA LAGASVISVL TEPTWFKGSL LDMRLARQAI DNLPHRPAIL 370 380 390 400 410 420 RKDFIIDEYQ IDEARLHGAD TVLLIVATLT EKRLEELYAY SQSLGMEPLV EVNNAKEMEI 430 440 450 460 470 480 ALKLGAKVIG VNNRNLHDFN VDMGTTSRLA EMVRERDVIL CALSGIKDAQ DVNTYVEQGV 490 500 510 520 530 540 GAVLVGESLM RAPDTRAFIR QLLSIPESEA KGKGKETTPL SRSCGIRTEE EALAAAEAGA 550 560 570 580 590 600 DMLGLMFVPK SKRYVSLEKA QQIAAAIHSR RLSKPVLTSG KTLENEPWFT AQQPPSRSFV 610 620 630 640 650 660 WRFAARPLLV GVFQNQPLSV YLTPCVPQLD LVQLHGSEPA ELAKHYPVPV IRVFHVSADG 670 680 690 700 710 720 RGLADLARPG LHQFALLDAV LPGSASALSG GTGTTVDWAL ARDAVRSGEV RVARSAQGDG 730 740 750 760 770 780 PVLSLNSSEA LYPMPVILAG GPQPENVSEA VDTVAPWAVD VSGGVELEDG SGKDLEKVRA FVKAAKKL

References

[1]

"The trpC gene of Phanerochaete chrysosporium is unique in containing an intron but nevertheless maintains the order of functional domains seen in other fungi." Schrank A., Tempelaars C., Sims P.F.G., Oliver S.G., Broda P. Mol. Microbiol. 5:467-476(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56047 Genomic DNA. Translation: CAA39518.1.
PIR	S15239.
3D structure databases
ProteinModelPortal	P25170.
ModBase	Search...
Protein-protein interaction databases
STRING	5306.JGI27842.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0134.
Enzyme and pathway databases
UniPathway	UPA00035; UER00040. UPA00035; UER00042. UPA00035; UER00043.
Family and domain databases
Gene3D	3.20.20.70. 3 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_PHACH

Accession

Primary (citable) accession number: P25170

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program