Q9T0J5 (ASE3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amidophosphoribosyltransferase 3, chloroplastic
Short name=AtATase3
Short name=PRPP3
EC=2.4.2.14

Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase 3
Short name=AtGPRAT3

Gene names

Name:	ASE3
Synonyms:	GPRAT3
Ordered Locus Names:	At4g38880
ORF Names:	F19H22.3, T9A14

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the first committed step of 'de novo' purine biosynthesis from glutamine. Ref.4
Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. Ref.4
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. Binds 1 magnesium ion per subunit By similarity.
Enzyme regulation	Inhibited by the phenyltriazole acetic acid compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid (DAS734), a bleaching herbicide. Repressed by AMP, ADP, ATP and GTP, and slightly by GMP. Ref.4
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Subcellular location	Plastid › chloroplast stroma By similarity.
Tissue specificity	Mostly expressed at low levels in leaves, and, to a lower extent, in cotyledons. Ref.3
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Glutamine amidotransferase Transit peptide
Ligand	Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding 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
	Transit peptide	1 – 59	59	Chloroplast Potential
	Chain	60 – 532	473	Amidophosphoribosyltransferase 3, chloroplastic		PRO_0000420283
Regions
	Domain	77 – 296	220	Glutamine amidotransferase type-2
Sites
	Active site	77	1	Nucleophile By similarity
	Metal binding	313	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	459	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	511	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	514	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9T0J5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C1B67B430D36A775	FASTA	532	58,041
	10 20 30 40 50 60 MAFSVEEISS ILPNSLSANP RNVSQNTISP SFFKPSLKPY ASKTLISLSC RRSLSPVFSA 70 80 90 100 110 120 GTYVTNVDED DKLHEECGVV GIHGDPEASR LSYLALHALQ HRGQEGAGIV AANQNGLESI 130 140 150 160 170 180 TGVGLVSDVF TESKLNNLPG DIAIGHVRYS TSGASMLKNV QPFIASCKLG SLAVAHNGNF 190 200 210 220 230 240 VNYKQLKTKL EEMGSIFITS SDTELVLHLI AKSKAKTFLL RVIDACEKLR GAYSMVFVFE 250 260 270 280 290 300 DKLIAVRDPF GFRPLVMGRR SNGAVVFASE TCALDLIDAT YEREVCPGEI VVVDRNHGDS 310 320 330 340 350 360 SMFMISHPEQ KQCVFEHGYF SQPNSIVFGR SVYETRRMYG EILATVAPVD CDVVIAVPDS 370 380 390 400 410 420 GTVAALGYAA KAGVPFQIGL LRSHYAKRTF IEPTQEIRDF AVKVKLSPVR AVLEGKRVVV 430 440 450 460 470 480 VDDSIVRGTT SLKIVRMLRD AGAKEVHMRI ALPPMIASCY YGVDTPRSQE LISSKMSVEA 490 500 510 520 530 IQKHINCDSL AFLPLDSLKG VYGPVESHRY CYACFTGKYP VTKTESEEAD AS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Characterization of Arabidopsis glutamine phosphoribosyl pyrophosphate amidotransferase-deficient mutants." Hung W.-F., Chen L.-J., Boldt R., Sun C.-W., Li H.-M. Plant Physiol. 135:1314-1323(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[4]	"Chemical genetic identification of glutamine phosphoribosylpyrophosphate amidotransferase as the target for a novel bleaching herbicide in Arabidopsis." Walsh T.A., Bauer T., Neal R., Merlo A.O., Schmitzer P.R., Hicks G.R., Honma M., Matsumura W., Wolff K., Davies J.P. Plant Physiol. 144:1292-1304(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL035656 Genomic DNA. Translation: CAB38622.1. AL161594 Genomic DNA. Translation: CAB80551.1. CP002687 Genomic DNA. Translation: AEE86986.1.
IPI	IPI00534892.
PIR	T06087.
RefSeq	NP_195599.1. NM_120048.1.
UniGene	At.54650.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ProteinModelPortal	Q9T0J5.
SMR	Q9T0J5. Positions 77-520.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G38880.1-P.
Protein family/group databases
MEROPS	C44.A02.
Proteomic databases
PaxDb	Q9T0J5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G38880.1; AT4G38880.1; AT4G38880.
GeneID	830043.
KEGG	ath:AT4G38880.
Organism-specific databases
GeneFarm	2376. 186.
TAIR	At4g38880.
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HOG000033688.
InParanoid	Q9T0J5.
KO	K00764.
OMA	HRGHEGV.
PhylomeDB	Q9T0J5.
ProtClustDB	PLN02440.
Enzyme and pathway databases
UniPathway	UPA00074; UER00124.
Gene expression databases
Genevestigator	Q9T0J5.
Family and domain databases
InterPro	IPR005854. Amd_phspho_trans. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR000836. PRibTrfase_dom. [Graphical view]
Pfam	PF13537. GATase_7. 1 hit. PF00156. Pribosyltran. 1 hit. [Graphical view]
PIRSF	PIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMs	TIGR01134. purF. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASE3_ARATH

Accession

Primary (citable) accession number: Q9T0J5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program