P24773 (TRPG_PENCH) 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

Penicillium chrysogenum (Penicillium notatum)

Taxonomic identifier

5076 [NCBI]

Taxonomic lineage

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

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.

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 – 752	752	Anthranilate synthase component 2		PRO_0000056862
Regions
	Domain	23 – 223	201	Glutamine amidotransferase type-1
	Region	239 – 503	265	Indole-3-glycerol phosphate synthase
	Region	519 – 752	234	N-(5'-phosphoribosyl)anthranilate isomerase
Sites
	Active site	102	1	For GATase activity By similarity
	Active site	197	1	For GATase activity By similarity
	Active site	199	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P24773 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: D6256C3818E22FDB	FASTA	752	81,035
	10 20 30 40 50 60 MADLVDHSPH HATKAAKLAS ASNVILIDNY DSFTWNIYQY LVLEGATVTV YRNDEVTVED 70 80 90 100 110 120 LVAKKPTQLV ISPGPGHPDT DAGISNAVIK HFSGKVPIFG VCMGQQCMIT SFGGKVDVTG 130 140 150 160 170 180 EILHGKTSEL KHDSKGVYQG LPTSLEVTRY HSLAGTHSTI PDCLEVTSRV ELGDASGKNI 190 200 210 220 230 240 IMGVRHKEFA VEGVQFHPES ILTQYGRKMF RNFLELTAGT WDNKQGAAVA APADKKLSIL 250 260 270 280 290 300 DKIYAHRKNA VDEQKKIPAL RPEALQAAYD LNIAPPQLSF PDRLRQSDYP LSLMAEIKRA 310 320 330 340 350 360 SPSKGIISAN VCAPAQAREY AKAGASVISV LTEPEWFKGT IDDLRAVRQS LEGLPNRPAV 370 380 390 400 410 420 LRKEFVFEEY QILEARLAGA DTVLLIVKML DIELLTRLYH YSRSLGMEPL VEVNTPEEMK 430 440 450 460 470 480 IAVDLGSEVI GVNNRDLTSF EVDLGTTSRL MDQVPESTIV CALSGISGPQ DVEAYKKEGV 490 500 510 520 530 540 KAILVGEALM RAPDTSAFVA QLLGGSNQNF AGASPSSPLV KICGTRTEEG ALAAIQAGAD 550 560 570 580 590 600 LIGIIMVQGR SRLVPDDVAL GISRVVKSTP RPADTLQQPS SATSLEWFDH STNILRHPSR 610 620 630 640 650 660 ALLVGVFMNQ PLSYVVSQQQ KLGLDVVQLH GSEPLEWSSL IPVPVIRKFA PGDIGIARRA 670 680 690 700 710 720 YHTLPLLDSG AGGSGELLEE SGVKKVLDSD EGLRVILAGG LNPDNVAGTV KKLGQSGQKV 730 740 750 VGLDVSSGVE TNGAQDLEKI RAFVKSAKSI RQ

References

[1]	"The complete nucleotide sequence of the trpC gene from Penicillium chrysogenum." Penalva M.A., Sanchez F. Nucleic Acids Res. 15:1874-1874(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X05033 Genomic DNA. Translation: CAA28707.1.
PIR	S30084.
3D structure databases
ProteinModelPortal	P24773.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
PhylomeDB	P24773.
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_PENCH

Accession

Primary (citable) accession number: P24773

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program