P05328 (TRPG_ASPNG) 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

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	770 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 – 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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69 AND 392-433.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07071 Genomic DNA. Translation: CAA30107.1. M14403 Genomic DNA. Translation: AAA32710.1. M14404 Genomic DNA. Translation: AAA32709.1.
PIR	S00643.
3D structure databases
ProteinModelPortal	P05328.
ModBase	Search...
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. IPR013798. Indole-3-glycerol_P_synth. IPR001468. Indole-3-GlycerolPSynthase_CS. IPR001240. PRAI_dom. IPR011060. RibuloseP-bd_barrel. IPR006221. TrpG/PapA_dom. [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_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:	May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program