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Q9T0J5 (ASE3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 93. 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 3, chloroplastic

Short name=AtATase3
Short name=PRPP3
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase 3
Short name=AtGPRAT3
Gene names
Name:ASE3
Synonyms:GPRAT3
Ordered Locus Names:At4g38880
ORF Names:F19H22.3, T9A14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length532 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. Ref.4

Catalytic activity

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. Ref.4

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. Repressed by AMP, ADP, ATP and GTP, and slightly by GMP. Ref.4

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 By similarity.

Tissue specificity

Mostly expressed at low levels in leaves, and, to a lower extent, in cotyledons. Ref.3

Sequence similarities

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

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Chloroplast Potential
Chain60 – 532473Amidophosphoribosyltransferase 3, chloroplastic
PRO_0000420283

Regions

Domain77 – 296220Glutamine amidotransferase type-2

Sites

Active site771Nucleophile By similarity
Metal binding3131Iron-sulfur (4Fe-4S) By similarity
Metal binding4591Iron-sulfur (4Fe-4S) By similarity
Metal binding5111Iron-sulfur (4Fe-4S) By similarity
Metal binding5141Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9T0J5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C1B67B430D36A775

FASTA53258,041
        10         20         30         40         50         60 
MAFSVEEISS ILPNSLSANP RNVSQNTISP SFFKPSLKPY ASKTLISLSC RRSLSPVFSA 

        70         80         90        100        110        120 
GTYVTNVDED DKLHEECGVV GIHGDPEASR LSYLALHALQ HRGQEGAGIV AANQNGLESI 

       130        140        150        160        170        180 
TGVGLVSDVF TESKLNNLPG DIAIGHVRYS TSGASMLKNV QPFIASCKLG SLAVAHNGNF 

       190        200        210        220        230        240 
VNYKQLKTKL EEMGSIFITS SDTELVLHLI AKSKAKTFLL RVIDACEKLR GAYSMVFVFE 

       250        260        270        280        290        300 
DKLIAVRDPF GFRPLVMGRR SNGAVVFASE TCALDLIDAT YEREVCPGEI VVVDRNHGDS 

       310        320        330        340        350        360 
SMFMISHPEQ KQCVFEHGYF SQPNSIVFGR SVYETRRMYG EILATVAPVD CDVVIAVPDS 

       370        380        390        400        410        420 
GTVAALGYAA KAGVPFQIGL LRSHYAKRTF IEPTQEIRDF AVKVKLSPVR AVLEGKRVVV 

       430        440        450        460        470        480 
VDDSIVRGTT SLKIVRMLRD AGAKEVHMRI ALPPMIASCY YGVDTPRSQE LISSKMSVEA 

       490        500        510        520        530 
IQKHINCDSL AFLPLDSLKG VYGPVESHRY CYACFTGKYP VTKTESEEAD AS 

« Hide

References

« Hide 'large scale' references
[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. 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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL035656 Genomic DNA. Translation: CAB38622.1.
AL161594 Genomic DNA. Translation: CAB80551.1.
CP002687 Genomic DNA. Translation: AEE86986.1.
PIRT06087.
RefSeqNP_195599.1. NM_120048.1.
UniGeneAt.54650.

3D structure databases

ProteinModelPortalQ9T0J5.
SMRQ9T0J5. Positions 77-530.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G38880.1-P.

Protein family/group databases

MEROPSC44.A02.

Proteomic databases

PaxDbQ9T0J5.
PRIDEQ9T0J5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G38880.1; AT4G38880.1; AT4G38880.
GeneID830043.
KEGGath:AT4G38880.

Organism-specific databases

GeneFarm2376. 186.
TAIRAT4G38880.

Phylogenomic databases

eggNOGCOG0034.
HOGENOMHOG000033688.
InParanoidQ9T0J5.
KOK00764.
OMALIRGTNI.
PhylomeDBQ9T0J5.
ProtClustDBPLN02440.

Enzyme and pathway databases

BioCycARA:AT4G38880-MONOMER.
UniPathwayUPA00074; UER00124.

Gene expression databases

GenevestigatorQ9T0J5.

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 nameASE3_ARATH
AccessionPrimary (citable) accession number: Q9T0J5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 93 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