Reviewed, UniProtKB/Swiss-Prot P00937 (TRPG_YEAST)

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 2 domains:
    1- Recommended name:
            Glutamine amidotransferase
    2- Recommended name:
            Indole-3-glycerol phosphate synthase
              EC=4.1.1.48
        Alternative name(s):
            PRAI

Gene names

Name:	TRP3
Ordered Locus Names:	YKL211C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O.
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 4/5.
Subunit structure	Tetramer of two components I and two components II.
Induction	By tryptophan starvation.
Miscellaneous	Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity. Yeast component II C-terminal half also has indole-3-glycerol phosphate synthase activity. Present with 13400 molecules/cell in log phase SD medium.
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	Lyase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: InterPro tryptophan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anthranilate synthase complex Inferred from physical interaction. Source: SGD
Molecular function	anthranilate synthase activity Inferred from electronic annotation. Source: InterPro indole-3-glycerol-phosphate synthase activity Ref.1 Inferred from electronic annotation. Source: InterPro 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 – 484	484	Anthranilate synthase component 2		PRO_0000056866
Regions
	Domain	13 – 207	195	Glutamine amidotransferase type-1
	Region	215 – 484	270	Indole-3-glycerol phosphate synthase
Sites
	Active site	92	1	For GATase activity By similarity
	Active site	181	1	For GATase activity By similarity
	Active site	183	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	2	1	Phosphoserine
	Modified residue	211	1	Phosphoserine
	Modified residue	444	1	Phosphoserine
Experimental info
	Sequence conflict	32	1	C → S in AAA34450. Ref.4
	Sequence conflict	63 – 65	3	PGP → LGL in AAA34450. Ref.4
	Sequence conflict	129	1	K → R in AAA35176. Ref.1
	Sequence conflict	170	1	H → Y in AAA34450. Ref.4
	Sequence conflict	236	1	G → S in AAA34450. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P00937-1 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 34EF65E829279C1F	FASTA	484	53,489
	10 20 30 40 50 60 MSVHAATNPI NKHVVLIDNY DSFTWNVYEY LCQEGAKVSV YRNDAITVPE IAALNPDTLL 70 80 90 100 110 120 ISPGPGHPKT DSGISRDCIR YFTGKIPVFG ICMGQQCMFD VFGGEVAYAG EIVHGKTSPI 130 140 150 160 170 180 SHDNCGIFKN VPQGIAVTRY HSLAGTESSL PSCLKVTAST ENGIIMGVRH KKYTVEGVQF 190 200 210 220 230 240 HPESILTEEG HLMIRNILNV SGGTWEENKS SPSNSILDRI YARRKIDVNE QSKIPGFTFQ 250 260 270 280 290 300 DLQSNYDLGL APPLQDFYTV LSSSHKRAVV LAEVKRASPS KGPICLKAVA AEQALKYAEA 310 320 330 340 350 360 GASAISVLTE PHWFHGSLQD LVNVRKILDL KFPPKERPCV LRKEFIFSKY QILEARLAGA 370 380 390 400 410 420 DTVLLIVKML SQPLLKELYS YSKDLNMEPL VEVNSKEELQ RALEIGAKVV GVNNRDLHSF 430 440 450 460 470 480 NVDLNTTSNL VESIPKDVLL IALSGITTRD DAEKYKKEGV HGFLVGEALM KSTDVKKFIH ELCE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3 encoding bifunctional anthranilate synthase: indole-3-glycerol phosphate synthase." Zalkin H., Paluh J.L., van Cleemput M., Moye W.S., Yanofsky C. J. Biol. Chem. 259:3985-3992(1984) [PubMed: 6323449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein." Tzermia M., Horaitis O., Alexandraki D. Yeast 10:663-679(1994) [PubMed: 7941750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Structure and function of the TRP3 gene of Saccharomyces cerevisiae: analysis of transcription, promoter sequence, and sequence coding for a glutamine amidotransferase." Aebi M., Furter R., Prantl F., Niederberger P., Huetter R. Curr. Genet. 8:165-172(1984) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-211 AND SER-444, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	K01386 Genomic DNA. Translation: AAA35176.1. X75951 Genomic DNA. Translation: CAA53562.1. Z28211 Genomic DNA. Translation: CAA82056.1. M36300 Genomic DNA. Translation: AAA34450.1.
PIR	NNBY2. S38049.
RefSeq	NP_012711.1.
3D structure databases
HSSP	HSSP built from PDB template 1I1Q based on UniProtKB P00905.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:543N.
Proteomic databases
PeptideAtlas	P00937.
Genome annotation databases
Ensembl	YKL211C. Saccharomyces cerevisiae. [Contig view]
GeneID	853669.
GenomeReviews	Gene locus YKL211C in contig Y13137_GR.
KEGG	sce:YKL211C.
NMPDR	fig|4932.3.peg.3689.
Organism-specific databases
CYGD	YKL211c.
SGD	S000001694. TRP3.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P00937.
Gene expression databases
ArrayExpress	P00937.
GermOnline	YKL211C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. IPR011702. GATASE. IPR012998. GATase_1_AS. IPR000991. GATase_class1_C. IPR013798. Indole-3-GPS. IPR001468. Indole-3-GPS_central. IPR006221. TrpG_papA. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00117. GATase. 1 hit. PF00218. IGPS. 1 hit. [Graphical view]
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...
Other Resources
LinkHub	P00937.
NextBio	974611.

Entry information

Entry name

TRPG_YEAST

Accession

Primary (citable) accession number: P00937

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 1, 1994
Last modified:	November 25, 2008
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)