Q92411 (TRPG_COCHE) 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

Organism

Cochliobolus heterostrophus (Drechslera maydis)

Taxonomic identifier

5016 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › dothideomyceta › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Pleosporaceae › Cochliobolus

Protein attributes

Sequence length	768 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 – 768	768	Anthranilate synthase component 2		PRO_0000056856
Regions
	Domain	25 – 225	201	Glutamine amidotransferase type-1
	Region	256 – 520	265	Indole-3-glycerol phosphate synthase
	Region	535 – 768	234	N-(5'-phosphoribosyl)anthranilate isomerase
Sites
	Active site	103	1	For GATase activity By similarity
	Active site	199	1	For GATase activity By similarity
	Active site	201	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92411 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: B2F215AA304B8B00	FASTA	768	83,655
	10 20 30 40 50 60 MPSSTLIDHS PRNPNPSPPR ITASNVILID NYDSFTWNVY QYLVFEGAFV TVYRNDEITL 70 80 90 100 110 120 DELIAKKPTQ LVISQVPDTR KEDVALAIEP LRTSVAKSPF SACAWESCIF YSYGGTVDVT 130 140 150 160 170 180 GQILHGKTCP LKHDGKGVFA GVPQDVPVTR YHSLAGTHGT LPDCLEISAT IPANADAEIK 190 200 210 220 230 240 EVIMGVRHKE YVIEGVQFHP ESILTEHGRL MMRNFLKMQG GTWAENERLQ KEAHAQAIGA 250 260 270 280 290 300 AFSESAMVQR TDSRTHLQKI YDHRRAAVAE QKKIPSNRPV DLQAAYDSNL APPQINFPER 310 320 330 340 350 360 LRQSPFKLSL MSEIKRASPS KGIISLSTCA PAQARLYAKA GARPISVLTE PEWFKGSIED 370 380 390 400 410 420 LRAVRQSIEG MANRPALLRK EFIFDEYQIL EGRLAGADTV LVIVKMLETE LLERLLGLSD 430 440 450 460 470 480 SVGMEPLVEV QNTDEMKIAV KLGAQVIGVN NRNLVNFEVD IGTTNRLIQM VPKETILCAL 490 500 510 520 530 540 SGIAGPKDVE AYIKDGVGAV LVGEALMRAS DMSQFISELL GGPYKEVRAS SSSPIVKISG 550 560 570 580 590 600 TRSEAAVAAV EAGADLIGII LAPGLKRTVT AETALSISEA VHKTKKPNVS KSGLLADSKT 610 620 630 640 650 660 ASDFFDHGAS RLLETISRAL LVGVFRNQSL EYVLEQQRLL NLDVVQLHGQ EPIEWAKLVP 670 680 690 700 710 720 VPVLKAFNPQ DHGIGTRGYH ALPLLDAGSG GSGKQLGLSD VKAAFTKDDG IKIILGRGLE 730 740 750 760 PDNVQTTLAG LDEYRDRVYA VDVSSGVEED GQQSLDKIRS FVKAAKSL

References

[1]	"Complementation of Cochliobolus heterostrophus trp-mutants produced by gene replacement." Mullin P.G., Turgeon B.G., Yoder O.C. Fungal Genet. Newsl. 40:51-53(1993) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 48330 / C3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70035 Genomic DNA. Translation: CAA49629.1.
3D structure databases
ProteinModelPortal	Q92411.
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. 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_COCHE

Accession

Primary (citable) accession number: Q92411

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	March 6, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program