Q9STG9 (ASE2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amidophosphoribosyltransferase 2, chloroplastic
Short name=AtATase2
Short name=AtPURF2
Short name=PRPP2
EC=2.4.2.14

Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase 2
Short name=AtGPRAT2
Protein CHLOROPLAST IMPORT APPARATUS 1
Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS

Gene names

Name:	ASE2
Synonyms:	CIA1, DOV1, GPRAT2, PURF2
Ordered Locus Names:	At4g34740
ORF Names:	T4L20.320

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	561 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. Required for chloroplast biogenesis and cell division. Confers sensitivity to the phenyltriazole acetic acid compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid (DAS734), a bleaching herbicide. Ref.6 Ref.7 Ref.8
Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. Ref.8
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. Ref.8
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 Ref.7 Ref.9 Ref.10 Ref.11.
Tissue specificity	Mostly expressed in leaves, and, to a lower extent, in cotyledons. Ref.5 Ref.6 Ref.7
Disruption phenotype	Strong growth retardation and severe chlorosis in leaves; white leaves, but green cotyledons. Leaves missing the palisade mesophyll layer, due to reduced cell number and size. Abnormal thylakoid membrane in chloroplasts, probably due to photo-oxidative damage. Defective in protein import into chloroplasts. Ref.6 Ref.7
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.
Biophysicochemical properties	Kinetic parameters: KM=1.34 mM for glutamine Ref.8

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 chloroplast organization Inferred from mutant phenotype PubMed 9550714. Source: TAIR 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 purine nucleotide biosynthetic process Inferred from mutant phenotype Ref.6. Source: TAIR
Cellular_component	chloroplast stroma Inferred from direct assay Ref.7Ref.10. Source: TAIR
Molecular_function	amidophosphoribosyltransferase activity Inferred from mutant phenotype Ref.6. Source: TAIR 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 – 53	53	Chloroplast Potential
	Chain	54 – 561	508	Amidophosphoribosyltransferase 2, chloroplastic		PRO_0000420282
Regions
	Domain	87 – 307	221	Glutamine amidotransferase type-2
Sites
	Active site	87	1	Nucleophile By similarity
	Metal binding	323	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	469	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	520	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	523	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Mutagenesis	187	1	H → T in cia1-2; small plants with white leaves showing an irregular mosaic of green sectors. Ref.7
	Mutagenesis	264	1	R → K: Strong resistance to the bleaching herbicides DAS073 and DAS734. Ref.8
	Mutagenesis	265	1	P → S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494. Ref.8
	Mutagenesis	371	1	G → S: Low resistance to the bleaching herbicides DAS073 and DAS734. Ref.8
	Mutagenesis	476	1	P → S: Resistance to the bleaching herbicides DAS073 and DAS734. Ref.8
	Mutagenesis	494	1	Y → F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265. Ref.8
	Sequence conflict	5	1	S → C in AAW28080. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9STG9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: AE52BD02CE304796	FASTA	561	61,030
	10 20 30 40 50 60 MAATSSISSS LSLNAKPNKL SNNNNNNKPH RFLRNPFLNP SSSSFSPLPA SISSSSSSPS 70 80 90 100 110 120 FPLRVSNPLT LLAADNDDYD EKPREECGVV GIYGDSEASR LCYLALHALQ HRGQEGAGIV 130 140 150 160 170 180 TVSKDKVLQT ITGVGLVSEV FSESKLDQLP GDIAIGHVRY STAGSSMLKN VQPFVAGYRF 190 200 210 220 230 240 GSVGVAHNGN LVNYTKLRAD LEENGSIFNT SSDTEVVLHL IAISKARPFF MRIVDACEKL 250 260 270 280 290 300 QGAYSMVFVT EDKLVAVRDP HGFRPLVMGR RSNGAVVFAS ETCALDLIEA TYEREVYPGE 310 320 330 340 350 360 VLVVDKDGVK CQCLMPHPEP KQCIFEHIYF SLPNSIVFGR SVYESRHVFG EILATESPVD 370 380 390 400 410 420 CDVVIAVPDS GVVAALGYAA KAGVAFQQGL IRSHYVGRTF IEPSQKIRDF GVKLKLSPVR 430 440 450 460 470 480 GVLEGKRVVV VDDSIVRGTT SSKIVRLLRE AGAKEVHMRI ASPPIIASCY YGVDTPSSNE 490 500 510 520 530 540 LISNRMSVDE IRDYIGCDSL AFLSFETLKK HLGEDSRSFC YACFTGDYPV KPTEDKVKRG 550 560 GDFIDDGLVG GIHNIEGGWV R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purine biosynthesis links chloroplast development and altered metal homeostasis in Arabidopsis thaliana." Maurer A., Rogers E.E. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. En-1.
[2]	"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.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Two amidophosphoribosyltransferase genes of Arabidopsis thaliana expressed in different organs." Ito T., Shiraishi H., Okada K., Shimura Y. Plant Mol. Biol. 26:529-533(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-561, TISSUE SPECIFICITY. Strain: cv. Landsberg erecta. Tissue: Flower, Leaf and Root.
[6]	"Molecular analysis of 'de novo' purine biosynthesis in solanaceous species and in Arabidopsis thaliana." van der Graaff E., Hooykaas P., Lein W., Lerchl J., Kunze G., Sonnewald U., Boldt R. Front. Biosci. 9:1803-1816(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY. Strain: cv. C24.
[7]	"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: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-187, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[8]	"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, MUTAGENESIS OF ARG-264; PRO-265; GLY-371; PRO-476 AND TYR-494, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. Strain: cv. Columbia.
[9]	"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins." Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N. Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering." Olinares P.D., Ponnala L., van Wijk K.J. Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY842241 Genomic DNA. Translation: AAW28080.1. AL023094 Genomic DNA. Translation: CAA18853.1. AL161586 Genomic DNA. Translation: CAB80191.1. CP002687 Genomic DNA. Translation: AEE86417.1. AY065123 mRNA. Translation: AAL38299.1. AY081611 mRNA. Translation: AAM10173.1. D28869 mRNA. Translation: BAA06024.1.
IPI	IPI00530207.
PIR	T05294.
RefSeq	NP_195200.1. NM_119640.2.
UniGene	At.21088.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ProteinModelPortal	Q9STG9.
SMR	Q9STG9. Positions 87-537.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9STG9. 4 interactions.
STRING	3702.AT4G34740.1-P.
Protein family/group databases
MEROPS	C44.A01.
Proteomic databases
PRIDE	Q9STG9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G34740.1; AT4G34740.1; AT4G34740.
GeneID	829626.
KEGG	ath:AT4G34740.
Organism-specific databases
GeneFarm	2374. 186.
TAIR	At4g34740.
Phylogenomic databases
eggNOG	COG0034.
HOGENOM	HOG000033688.
InParanoid	Q9STG9.
KO	K00764.
OMA	LAFLSFE.
PhylomeDB	Q9STG9.
ProtClustDB	PLN02440.
Enzyme and pathway databases
UniPathway	UPA00074; UER00124.
Gene expression databases
ArrayExpress	Q9STG9.
Genevestigator	Q9STG9.
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

ASE2_ARATH

Accession

Primary (citable) accession number: Q9STG9
Secondary accession number(s): Q39000, Q5MAT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program