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Q9STG9

- ASE2_ARATH

UniProt

Q9STG9 - ASE2_ARATH

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Protein
Amidophosphoribosyltransferase 2, chloroplastic
Gene
ASE2, CIA1, DOV1, GPRAT2, PURF2, At4g34740, T4L20.320
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.1 Publication

Cofactori

Binds 1 4Fe-4S cluster per subunit By similarity.
Binds 1 magnesium ion per subunit By similarity.

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=1.34 mM for glutamine1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Nucleophile By similarity
Metal bindingi323 – 3231Iron-sulfur (4Fe-4S) By similarity
Metal bindingi469 – 4691Iron-sulfur (4Fe-4S) By similarity
Metal bindingi520 – 5201Iron-sulfur (4Fe-4S) By similarity
Metal bindingi523 – 5231Iron-sulfur (4Fe-4S) By similarity

GO - Molecular functioni

  1. amidophosphoribosyltransferase activity Source: TAIR
  2. iron-sulfur cluster binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. chloroplast organization Source: TAIR
  3. glutamine metabolic process Source: UniProtKB-KW
  4. nucleoside metabolic process Source: InterPro
  5. purine nucleobase biosynthetic process Source: InterPro
  6. purine nucleotide biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G34740-MONOMER.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.A01.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase 2, chloroplastic (EC:2.4.2.14)
Short name:
AtATase2
Short name:
AtPURF2
Short name:
PRPP2
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase 2
Short name:
AtGPRAT2
Protein CHLOROPLAST IMPORT APPARATUS 1
Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS
Gene namesi
Name:ASE2
Synonyms:CIA1, DOV1, GPRAT2, PURF2
Ordered Locus Names:At4g34740
ORF Names:T4L20.320
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G34740.

Subcellular locationi

Plastidchloroplast stroma 4 Publications

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
  3. plastid stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871H → T in cia1-2; small plants with white leaves showing an irregular mosaic of green sectors. 1 Publication
Mutagenesisi264 – 2641R → K: Strong resistance to the bleaching herbicides DAS073 and DAS734. 1 Publication
Mutagenesisi265 – 2651P → S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494. 1 Publication
Mutagenesisi371 – 3711G → S: Low resistance to the bleaching herbicides DAS073 and DAS734. 1 Publication
Mutagenesisi476 – 4761P → S: Resistance to the bleaching herbicides DAS073 and DAS734. 1 Publication
Mutagenesisi494 – 4941Y → F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5353Chloroplast Reviewed prediction
Add
BLAST
Chaini54 – 561508Amidophosphoribosyltransferase 2, chloroplastic
PRO_0000420282Add
BLAST

Proteomic databases

PRIDEiQ9STG9.

Expressioni

Tissue specificityi

Mostly expressed in leaves, and, to a lower extent, in cotyledons.3 Publications

Gene expression databases

GenevestigatoriQ9STG9.

Interactioni

Protein-protein interaction databases

IntActiQ9STG9. 4 interactions.
STRINGi3702.AT4G34740.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9STG9.
SMRiQ9STG9. Positions 87-537.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 307221Glutamine amidotransferase type-2
Add
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Keywords - Domaini

Glutamine amidotransferase, Transit peptide

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
InParanoidiQ9STG9.
KOiK00764.
OMAiIRDYIGC.
PhylomeDBiQ9STG9.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF13537. GATase_7. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9STG9-1 [UniParc]FASTAAdd to Basket

« Hide

MAATSSISSS LSLNAKPNKL SNNNNNNKPH RFLRNPFLNP SSSSFSPLPA    50
SISSSSSSPS FPLRVSNPLT LLAADNDDYD EKPREECGVV GIYGDSEASR 100
LCYLALHALQ HRGQEGAGIV TVSKDKVLQT ITGVGLVSEV FSESKLDQLP 150
GDIAIGHVRY STAGSSMLKN VQPFVAGYRF GSVGVAHNGN LVNYTKLRAD 200
LEENGSIFNT SSDTEVVLHL IAISKARPFF MRIVDACEKL QGAYSMVFVT 250
EDKLVAVRDP HGFRPLVMGR RSNGAVVFAS ETCALDLIEA TYEREVYPGE 300
VLVVDKDGVK CQCLMPHPEP KQCIFEHIYF SLPNSIVFGR SVYESRHVFG 350
EILATESPVD CDVVIAVPDS GVVAALGYAA KAGVAFQQGL IRSHYVGRTF 400
IEPSQKIRDF GVKLKLSPVR GVLEGKRVVV VDDSIVRGTT SSKIVRLLRE 450
AGAKEVHMRI ASPPIIASCY YGVDTPSSNE LISNRMSVDE IRDYIGCDSL 500
AFLSFETLKK HLGEDSRSFC YACFTGDYPV KPTEDKVKRG GDFIDDGLVG 550
GIHNIEGGWV R 561
Length:561
Mass (Da):61,030
Last modified:May 1, 2000 - v1
Checksum:iAE52BD02CE304796
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → C in AAW28080. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT05294.
RefSeqiNP_195200.1. NM_119640.2.
UniGeneiAt.21088.

Genome annotation databases

EnsemblPlantsiAT4G34740.1; AT4G34740.1; AT4G34740.
GeneIDi829626.
KEGGiath:AT4G34740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T05294.
RefSeqi NP_195200.1. NM_119640.2.
UniGenei At.21088.

3D structure databases

ProteinModelPortali Q9STG9.
SMRi Q9STG9. Positions 87-537.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9STG9. 4 interactions.
STRINGi 3702.AT4G34740.1-P.

Protein family/group databases

MEROPSi C44.A01.

Proteomic databases

PRIDEi Q9STG9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G34740.1 ; AT4G34740.1 ; AT4G34740 .
GeneIDi 829626.
KEGGi ath:AT4G34740.

Organism-specific databases

GeneFarmi 2374. 186.
TAIRi AT4G34740.

Phylogenomic databases

eggNOGi COG0034.
HOGENOMi HOG000033688.
InParanoidi Q9STG9.
KOi K00764.
OMAi IRDYIGC.
PhylomeDBi Q9STG9.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00124 .
BioCyci ARA:AT4G34740-MONOMER.

Gene expression databases

Genevestigatori Q9STG9.

Family and domain databases

Gene3Di 3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view ]
Pfami PF13537. GATase_7. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view ]
PIRSFi PIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMi SSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01134. purF. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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].
  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.

Entry informationi

Entry nameiASE2_ARATH
AccessioniPrimary (citable) accession number: Q9STG9
Secondary accession number(s): Q39000, Q5MAT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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