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Protein

Amidophosphoribosyltransferase 3, chloroplastic

Gene

ASE3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity
  • Mg2+By similarityNote: Binds 1 Mg2+ 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

Pathway:iIMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase 2, chloroplastic (ASE2), Amidophosphoribosyltransferase 1, chloroplastic (ASE1), Amidophosphoribosyltransferase 3, chloroplastic (ASE3)
  2. Phosphoribosylamine--glycine ligase, chloroplastic (PUR2)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

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

GO - Biological processi

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.
BRENDAi2.4.2.14. 399.
ReactomeiREACT_350544. Purine ribonucleoside monophosphate biosynthesis.
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 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G38880.

Subcellular locationi

GO - Cellular componenti

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

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G38880.1.

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.
OMAiLMHRGHE.
PhylomeDBiQ9T0J5.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi3702.AT4G38880.1.

Protein family/group databases

MEROPSiC44.A02.

Proteomic databases

PaxDbiQ9T0J5.
PRIDEiQ9T0J5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GeneFarmi2376. 186.
TAIRiAT4G38880.

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
InParanoidiQ9T0J5.
KOiK00764.
OMAiLMHRGHE.
PhylomeDBiQ9T0J5.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
BioCyciARA:AT4G38880-MONOMER.
BRENDAi2.4.2.14. 399.
ReactomeiREACT_350544. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiQ9T0J5.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[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]
ProtoNetiSearch...

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: July 22, 2015
This is version 103 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.