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Q9STG9 (ASE2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Plastidchloroplast 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Chloroplast Potential
Chain54 – 561508Amidophosphoribosyltransferase 2, chloroplastic
PRO_0000420282

Regions

Domain87 – 307221Glutamine amidotransferase type-2

Sites

Active site871Nucleophile By similarity
Metal binding3231Iron-sulfur (4Fe-4S) By similarity
Metal binding4691Iron-sulfur (4Fe-4S) By similarity
Metal binding5201Iron-sulfur (4Fe-4S) By similarity
Metal binding5231Iron-sulfur (4Fe-4S) By similarity

Experimental info

Mutagenesis1871H → T in cia1-2; small plants with white leaves showing an irregular mosaic of green sectors. Ref.7
Mutagenesis2641R → K: Strong resistance to the bleaching herbicides DAS073 and DAS734. Ref.8
Mutagenesis2651P → S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494. Ref.8
Mutagenesis3711G → S: Low resistance to the bleaching herbicides DAS073 and DAS734. Ref.8
Mutagenesis4761P → S: Resistance to the bleaching herbicides DAS073 and DAS734. Ref.8
Mutagenesis4941Y → F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265. Ref.8
Sequence conflict51S → C in AAW28080. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9STG9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AE52BD02CE304796

FASTA56161,030
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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].
[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].
[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].
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.
PIRT05294.
RefSeqNP_195200.1. NM_119640.2.
UniGeneAt.21088.

3D structure databases

ProteinModelPortalQ9STG9.
SMRQ9STG9. Positions 87-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9STG9. 4 interactions.
STRING3702.AT4G34740.1-P.

Protein family/group databases

MEROPSC44.A01.

Proteomic databases

PRIDEQ9STG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G34740.1; AT4G34740.1; AT4G34740.
GeneID829626.
KEGGath:AT4G34740.

Organism-specific databases

GeneFarm2374. 186.
TAIRAT4G34740.

Phylogenomic databases

eggNOGCOG0034.
HOGENOMHOG000033688.
InParanoidQ9STG9.
KOK00764.
OMATESPVDC.
PhylomeDBQ9STG9.
ProtClustDBPLN02440.

Enzyme and pathway databases

BioCycARA:AT4G34740-MONOMER.
UniPathwayUPA00074; UER00124.

Gene expression databases

GenevestigatorQ9STG9.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF13537. GATase_7. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASE2_ARATH
AccessionPrimary (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: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names