Reviewed, UniProtKB/Swiss-Prot P05328 (TRPG_ASPNG)

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

Gene names

Name:

trpC

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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-KW
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 – 770	770	Anthranilate synthase component 2		PRO_0000056855
Regions
	Domain	25 – 225	201	Glutamine amidotransferase type-1
	Region	255 – 519	265	Indole-3-glycerol phosphate synthase
	Region	535 – 770	236	N-(5'-phosphoribosyl)anthranilate isomerase
Sites
	Active site	104	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)
	P05328-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 36D8DE5B23097012	FASTA	770	82,910
	10 20 30 40 50 60 MADSGLVDHS PHHPTKAAQL STASNVILID NYDSFTWNVY QYLVLEGATV NVFRNDQITL 70 80 90 100 110 120 EELIAKKPTQ LVISPGPGHP ETDAGISSAA IQYFSGKIPI FGVCMGQQCI ITCFGGKVDV 130 140 150 160 170 180 TGEILHGKTS PLKHDGKGAY EGLPGSLAVT RYHSLAGTHA TIPDCLEVSS SVQLADDSNK 190 200 210 220 230 240 DVIMGVRHKK LAVEGVQFHP ESILTEYGRI MFRNFLKLTA GTWEGNGKHF GEQSSTTKAT 250 260 270 280 290 300 VPSNPPPKTD KKLSILERIY DHRRAAVAVQ KTIPSQRPAD LQAAYDLNLA PPQIPFPARL 310 320 330 340 350 360 RQSPYPLSLM AEIKRASPSK GMIAENACAP AQARQYAKAG ASVISVLTEP EWFKGSIDDL 370 380 390 400 410 420 RAVRQSLEGM TNRPAILRKE FVFDEYQILE ARLAGADTVL LIVKMLSVEL LTRLYHYSRS 430 440 450 460 470 480 LGMEPLVEVN TPEEMKIAVD LGAEVIGVNN RDLTSFEVDL GTTSRLMDQV PSSTIVCALS 490 500 510 520 530 540 GISGPKDVEA YKKEGVKAIL VGEALMRAAD TATFIAELLG GSSQTVSSES RRSPLVKICG 550 560 570 580 590 600 TRSEEAARAA IEAGADLIGI IMVQGRTGCV PDDVALPISQ VVRSTPKPAS QALHTSQEPP 610 620 630 640 650 660 AATSVEYFDH SAKILRHPSR ALLVGVFQNQ PLDYILSQQQ KLGLDVVQLH GSEPLEWAKL 670 680 690 700 710 720 IPVPVIRKFG LDEPAIARRA YHSLPLLDSG VGGTGELLDQ SRVQNVLDKD CGLRVILAGG 730 740 750 760 770 LDPTNVAGIV QKLGESGRKV VGVDVSSGVE SDGAQDLNKI RAFVQAVRGL

References

[1]	"Nucleotide sequence of the Aspergillus niger trpC gene: structural relationship with analogous genes of other organisms." Kos T., Kuijvenhoven A., Hessing H.G.M., Pouwels P.H., van den Hondel C.A.M.J.J. Curr. Genet. 13:137-144(1988) [PubMed: 2836085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 401.
[2]	"Isolation and characterization of the Aspergillus niger trpC gene." Kos A., Kuijvenhoven J., Wernars K., Bos C.J., van den Broek H.W.J., Pouwels P.H., van den Hondel C.A.M.J.J. Gene 39:231-238(1985) [PubMed: 2936650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69 AND 392-433.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X07071 Genomic DNA. Translation: CAA30107.1. M14403 Genomic DNA. Translation: AAA32710.1. M14404 Genomic DNA. Translation: AAA32709.1.
PIR	S00643.
3D structure databases
HSSP	HSSP built from PDB template 1I1Q based on UniProtKB P00905.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.48. 277. 4.1.3.27. 277. 5.3.1.24. 277.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006220. Anth_synthII. IPR016302. Anthranilate_synth_II_fun. IPR001317. CarbamoylP_synth_GATase. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GPS_central. IPR001240. PRAI. IPR006221. TrpG_papA. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
Pfam	PF00117. GATase. 1 hit. PF00218. IGPS. 1 hit. PF00697. PRAI. 1 hit. [Graphical view]
PIRSF	PIRSF001382. TrpG-trpC-trpF. 1 hit.
PRINTS	PR00097. ANTSNTHASEII. PR00099. CPSGATASE. PR00096. GATASE.
ProDom	PD001511. IGPS. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_ASPNG

Accession

Primary (citable) accession number: P05328

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)