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Q9T0J5

- ASE3_ARATH

UniProt

Q9T0J5 - ASE3_ARATH

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Protein

Amidophosphoribosyltransferase 3, chloroplastic

Gene

ASE3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the first committed step of 'de novo' purine biosynthesis from glutamine.1 Publication

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. Repressed by AMP, ADP, ATP and GTP, and slightly by GMP.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei77 – 771NucleophilePROSITE-ProRule annotation
Metal bindingi313 – 3131Iron-sulfur (4Fe-4S)By similarity
Metal bindingi459 – 4591Iron-sulfur (4Fe-4S)By similarity
Metal bindingi511 – 5111Iron-sulfur (4Fe-4S)By similarity
Metal bindingi514 – 5141Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  1. amidophosphoribosyltransferase activity Source: UniProtKB-EC
  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. glutamine metabolic process Source: UniProtKB-KW
  3. nucleoside metabolic process Source: InterPro
  4. purine nucleobase biosynthetic process Source: InterPro
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:AT4G38880-MONOMER.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase 3, chloroplastic (EC:2.4.2.14)
Short name:
AtATase3
Short name:
PRPP3
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase 3
Short name:
AtGPRAT3
Gene namesi
Name:ASE3
Synonyms:GPRAT3
Ordered Locus Names:At4g38880
ORF Names:F19H22.3, T9A14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G38880.

Subcellular locationi

Plastidchloroplast stroma By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959ChloroplastSequence AnalysisAdd
BLAST
Chaini60 – 532473Amidophosphoribosyltransferase 3, chloroplasticPRO_0000420283Add
BLAST

Proteomic databases

PaxDbiQ9T0J5.
PRIDEiQ9T0J5.

Expressioni

Tissue specificityi

Mostly expressed at low levels in leaves, and, to a lower extent, in cotyledons.1 Publication

Gene expression databases

GenevestigatoriQ9T0J5.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G38880.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9T0J5.
SMRiQ9T0J5. Positions 77-520.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 296220Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase, Transit peptide

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
InParanoidiQ9T0J5.
KOiK00764.
OMAiPFIASCK.
PhylomeDBiQ9T0J5.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
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.

Q9T0J5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFSVEEISS ILPNSLSANP RNVSQNTISP SFFKPSLKPY ASKTLISLSC
60 70 80 90 100
RRSLSPVFSA GTYVTNVDED DKLHEECGVV GIHGDPEASR LSYLALHALQ
110 120 130 140 150
HRGQEGAGIV AANQNGLESI TGVGLVSDVF TESKLNNLPG DIAIGHVRYS
160 170 180 190 200
TSGASMLKNV QPFIASCKLG SLAVAHNGNF VNYKQLKTKL EEMGSIFITS
210 220 230 240 250
SDTELVLHLI AKSKAKTFLL RVIDACEKLR GAYSMVFVFE DKLIAVRDPF
260 270 280 290 300
GFRPLVMGRR SNGAVVFASE TCALDLIDAT YEREVCPGEI VVVDRNHGDS
310 320 330 340 350
SMFMISHPEQ KQCVFEHGYF SQPNSIVFGR SVYETRRMYG EILATVAPVD
360 370 380 390 400
CDVVIAVPDS GTVAALGYAA KAGVPFQIGL LRSHYAKRTF IEPTQEIRDF
410 420 430 440 450
AVKVKLSPVR AVLEGKRVVV VDDSIVRGTT SLKIVRMLRD AGAKEVHMRI
460 470 480 490 500
ALPPMIASCY YGVDTPRSQE LISSKMSVEA IQKHINCDSL AFLPLDSLKG
510 520 530
VYGPVESHRY CYACFTGKYP VTKTESEEAD AS
Length:532
Mass (Da):58,041
Last modified:May 1, 2000 - v1
Checksum:iC1B67B430D36A775
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL035656 Genomic DNA. Translation: CAB38622.1.
AL161594 Genomic DNA. Translation: CAB80551.1.
CP002687 Genomic DNA. Translation: AEE86986.1.
PIRiT06087.
RefSeqiNP_195599.1. NM_120048.1.
UniGeneiAt.54650.

Genome annotation databases

EnsemblPlantsiAT4G38880.1; AT4G38880.1; AT4G38880.
GeneIDi830043.
KEGGiath:AT4G38880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL035656 Genomic DNA. Translation: CAB38622.1 .
AL161594 Genomic DNA. Translation: CAB80551.1 .
CP002687 Genomic DNA. Translation: AEE86986.1 .
PIRi T06087.
RefSeqi NP_195599.1. NM_120048.1.
UniGenei At.54650.

3D structure databases

ProteinModelPortali Q9T0J5.
SMRi Q9T0J5. Positions 77-520.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G38880.1-P.

Protein family/group databases

MEROPSi C44.A02.

Proteomic databases

PaxDbi Q9T0J5.
PRIDEi Q9T0J5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G38880.1 ; AT4G38880.1 ; AT4G38880 .
GeneIDi 830043.
KEGGi ath:AT4G38880.

Organism-specific databases

GeneFarmi 2376. 186.
TAIRi AT4G38880.

Phylogenomic databases

eggNOGi COG0034.
HOGENOMi HOG000033688.
InParanoidi Q9T0J5.
KOi K00764.
OMAi PFIASCK.
PhylomeDBi Q9T0J5.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00124 .
BioCyci ARA:AT4G38880-MONOMER.

Gene expression databases

Genevestigatori Q9T0J5.

Family and domain databases

Gene3Di 3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPi MF_01931. PurF.
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. "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.

Entry informationi

Entry nameiASE3_ARATH
AccessioniPrimary (citable) accession number: Q9T0J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 97 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