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Protein

Amidophosphoribosyltransferase 1, chloroplastic

Gene

ASE1

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

Functioni

Catalyzes the first committed step of 'de novo' purine biosynthesis from glutamine. Involved in plastid biogenesis and cell division.1 Publication

Catalytic activityi

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

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

Pathway: IMP 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 sitei91 – 911NucleophilePROSITE-ProRule annotation
Metal bindingi327 – 3271Iron-sulfur (4Fe-4S)By similarity
Metal bindingi473 – 4731Iron-sulfur (4Fe-4S)By similarity
Metal bindingi524 – 5241Iron-sulfur (4Fe-4S)By similarity
Metal bindingi527 – 5271Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  • amidophosphoribosyltransferase activity Source: TAIR
  • iron-sulfur cluster binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

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:AT2G16570-MONOMER.
BRENDAi2.4.2.14. 399.
ReactomeiREACT_350544. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.A01.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase 1, chloroplastic (EC:2.4.2.14)
Short name:
AtATase1
Short name:
PRPP1
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase 1
Short name:
AtGPRAT1
Gene namesi
Name:ASE1
Synonyms:GPRAT1
Ordered Locus Names:At2g16570
ORF Names:F1P15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G16570.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: TAIR
  • plastid Source: TAIR
  • plastid stroma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5858ChloroplastSequence AnalysisAdd
BLAST
Chaini59 – 566508Amidophosphoribosyltransferase 1, chloroplasticPRO_0000420281Add
BLAST

Proteomic databases

PRIDEiQ9SI61.

Expressioni

Tissue specificityi

Expressed in flowers and roots. Also present in leaves, and, to a lower extent, in cotyledons.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi1514. 1 interaction.
IntActiQ9SI61. 1 interaction.
STRINGi3702.AT2G16570.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SI61.
SMRiQ9SI61. Positions 91-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 311221Glutamine 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.
InParanoidiQ9SI61.
KOiK00764.
OMAiIEVHIRI.
PhylomeDBiQ9SI61.

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]
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.

Q9SI61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATTSFSSS LSLITKPNNS SYTNQPLPLF PKPFLKPPHL SLLPSPLSSP
60 70 80 90 100
PPSLIHGVSS YFSSPSPSED NSHTPFDYHN DEDDEKPREE CGVVGIYGDP
110 120 130 140 150
EASRLCYLAL HALQHRGQEG AGIVTVSPEK VLQTITGVGL VSEVFNESKL
160 170 180 190 200
DQLPGEFAIG HVRYSTAGAS MLKNVQPFVA GYRFGSIGVA HNGNLVNYKT
210 220 230 240 250
LRAMLEENGS IFNTSSDTEV VLHLIAISKA RPFFMRIIDA CEKLQGAYSM
260 270 280 290 300
VFVTEDKLVA VRDPYGFRPL VMGRRSNGAV VFASETCALD LIEATYEREV
310 320 330 340 350
YPGEVLVVDK DGVKSQCLMP KFEPKQCIFE HIYFSLPNSI VFGRSVYESR
360 370 380 390 400
HVFGEILATE SPVECDVVIA VPDSGVVAAL GYAAKSGVPF QQGLIRSHYV
410 420 430 440 450
GRTFIEPSQK IRDFGVKLKL SPVRGVLEGK RVVVVDDSIV RGTTSSKIVR
460 470 480 490 500
LLREAGAKEV HMRIASPPIV ASCYYGVDTP SSEELISNRL SVEEINEFIG
510 520 530 540 550
SDSLAFLSFD TLKKHLGKDS KSFCYACFTG DYPVKPTEVK VKRGGGDFID
560
DGLVGSFENI EAGWVR
Length:566
Mass (Da):61,842
Last modified:May 1, 2000 - v1
Checksum:i887827A9FEB901E0
GO

Sequence cautioni

The sequence BAA06023.1 differs from that shown. Reason: Frameshift at position 70. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741T → A in BAA06023 (PubMed:7948903).Curated
Sequence conflicti106 – 1061C → F in BAA06023 (PubMed:7948903).Curated
Sequence conflicti160 – 1601G → A in BAA06023 (PubMed:7948903).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28868 mRNA. Translation: BAA06023.1. Frameshift.
AC007195 Genomic DNA. Translation: AAD26498.1.
CP002685 Genomic DNA. Translation: AEC06510.1.
PIRiE84541.
S52622.
RefSeqiNP_179247.1. NM_127208.1.
UniGeneiAt.14491.

Genome annotation databases

EnsemblPlantsiAT2G16570.1; AT2G16570.1; AT2G16570.
GeneIDi816156.
KEGGiath:AT2G16570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28868 mRNA. Translation: BAA06023.1. Frameshift.
AC007195 Genomic DNA. Translation: AAD26498.1.
CP002685 Genomic DNA. Translation: AEC06510.1.
PIRiE84541.
S52622.
RefSeqiNP_179247.1. NM_127208.1.
UniGeneiAt.14491.

3D structure databases

ProteinModelPortaliQ9SI61.
SMRiQ9SI61. Positions 91-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1514. 1 interaction.
IntActiQ9SI61. 1 interaction.
STRINGi3702.AT2G16570.1.

Protein family/group databases

MEROPSiC44.A01.

Proteomic databases

PRIDEiQ9SI61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G16570.1; AT2G16570.1; AT2G16570.
GeneIDi816156.
KEGGiath:AT2G16570.

Organism-specific databases

GeneFarmi2372. 186.
TAIRiAT2G16570.

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
InParanoidiQ9SI61.
KOiK00764.
OMAiIEVHIRI.
PhylomeDBiQ9SI61.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
BioCyciARA:AT2G16570-MONOMER.
BRENDAi2.4.2.14. 399.
ReactomeiREACT_350544. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiQ9SI61.

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]
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. "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], TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
    Tissue: Flower and Root.
  2. 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. "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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiASE1_ARATH
AccessioniPrimary (citable) accession number: Q9SI61
Secondary accession number(s): Q38999
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 99 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.