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Protein

Amidophosphoribosyltransferase 1, chloroplastic

Gene

ASE1

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

Pathwayi: 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 (AXX17_At4g39730), Amidophosphoribosyltransferase 1, chloroplastic (ASE1), Amidophosphoribosyltransferase 3, chloroplastic (ASE3), Amidophosphoribosyltransferase (AXX17_At4g44210), Amidophosphoribosyltransferase (AXX17_At2g11630)
  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)DescriptionActionsGraphical viewLength
Active sitei91NucleophilePROSITE-ProRule annotation1
Metal bindingi327Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi473Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi524Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi527Iron-sulfur (4Fe-4S)By similarity1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processPurine biosynthesis
LigandIron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT2G16570-MONOMER
BRENDAi2.4.2.14 399
ReactomeiR-ATH-73817 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
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

AraportiAT2G16570
TAIRilocus:2045081 AT2G16570

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 58ChloroplastSequence analysisAdd BLAST58
ChainiPRO_000042028159 – 566Amidophosphoribosyltransferase 1, chloroplasticAdd BLAST508

Proteomic databases

PaxDbiQ9SI61

PTM databases

SwissPalmiQ9SI61

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiQ9SI61 baseline and differential
GenevisibleiQ9SI61 AT

Interactioni

Protein-protein interaction databases

BioGridi1514, 1 interactor
IntActiQ9SI61, 1 interactor
STRINGi3702.AT2G16570.1

Structurei

3D structure databases

ProteinModelPortaliQ9SI61
SMRiQ9SI61
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 311Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST221

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase, Transit peptide

Phylogenomic databases

eggNOGiKOG0572 Eukaryota
COG0034 LUCA
HOGENOMiHOG000033688
InParanoidiQ9SI61
KOiK00764
OMAiFRPLCLG
OrthoDBiEOG093609B8
PhylomeDBiQ9SI61

Family and domain databases

CDDicd00715 GPATase_N, 1 hit
cd06223 PRTases_typeI, 1 hit
Gene3Di3.60.20.10, 3 hits
HAMAPiMF_01931 PurF, 1 hit
InterProiView protein in InterPro
IPR017932 GATase_2_dom
IPR029055 Ntn_hydrolases_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005854 PurF
IPR035584 PurF_N
PfamiView protein in Pfam
PF13537 GATase_7, 1 hit
PF00156 Pribosyltran, 1 hit
PIRSFiPIRSF000485 Amd_phspho_trans, 1 hit
SUPFAMiSSF53271 SSF53271, 1 hit
SSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR01134 purF, 1 hit
PROSITEiView protein in PROSITE
PS51278 GATASE_TYPE_2, 1 hit
PS00103 PUR_PYR_PR_TRANSFER, 1 hit

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 differs from that shown. Reason: Frameshift at position 70.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74T → A in BAA06023 (PubMed:7948903).Curated1
Sequence conflicti106C → F in BAA06023 (PubMed:7948903).Curated1
Sequence conflicti160G → A in BAA06023 (PubMed:7948903).Curated1

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_127208.2

Genome annotation databases

EnsemblPlantsiAT2G16570.1; AT2G16570.1; AT2G16570
GeneIDi816156
GrameneiAT2G16570.1; AT2G16570.1; AT2G16570
KEGGiath:AT2G16570

Similar proteinsi

Entry informationi

Entry nameiASE1_ARATH
AccessioniPrimary (citable) accession number: Q9SI61
Secondary accession number(s): Q38999
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: May 1, 2000
Last modified: April 25, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health