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Protein

Adenylosuccinate synthetase, chloroplastic

Gene

PURA

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

Functioni

Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

Catalytic activityi

GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic (PURA), Adenylosuccinate synthetase, chloroplastic (PURA)
  2. Adenylosuccinate lyase (At1g36280), Adenylosuccinate lyase (AXX17_At1g37010), Adenylosuccinate lyase (At1g36280), Adenylosuccinate lyase (F15C21.8), Adenylosuccinate lyase (AXX17_At4g21680), Adenylosuccinate lyase (At4g18440)
This subpathway is part of the pathway AMP 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 AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei78Proton acceptorUniRule annotation1
Metal bindingi78MagnesiumUniRule annotation1
Metal bindingi105Magnesium; via carbonyl oxygenUniRule annotation1
Active sitei106Proton donorUniRule annotation1
Binding sitei195IMPUniRule annotation1
Binding sitei209IMP; shared with dimeric partnerUniRule annotation1
Binding sitei289IMPUniRule annotation1
Binding sitei304IMPUniRule annotation1
Binding sitei368IMPUniRule annotation1
Binding sitei370GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi77 – 83GTP7
Nucleotide bindingi105 – 107GTP3
Nucleotide bindingi396 – 398GTP3
Nucleotide bindingi479 – 481GTP3

GO - Molecular functioni

GO - Biological processi

  • 'de novo' AMP biosynthetic process Source: GO_Central
  • IMP metabolic process Source: GO_Central
  • response to cadmium ion Source: TAIR

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G57610-MONOMER
MetaCyc:AT3G57610-MONOMER
BRENDAi6.3.4.4 399
ReactomeiR-ATH-73817 Purine ribonucleoside monophosphate biosynthesis
UniPathwayiUPA00075; UER00335

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate synthetase, chloroplasticUniRule annotation (EC:6.3.4.4UniRule annotation)
Short name:
AMPSaseUniRule annotation
Short name:
AdSSUniRule annotation
Alternative name(s):
IMP--aspartate ligaseUniRule annotation
Gene namesi
Name:PURAUniRule annotation
Ordered Locus Names:At3g57610
ORF Names:F15B8.200
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G57610
TAIRilocus:2076606 AT3G57610

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 – 45ChloroplastCombined sourcesAdd BLAST45
ChainiPRO_000002987046 – 490Adenylosuccinate synthetase, chloroplasticAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ96529
PRIDEiQ96529

PTM databases

iPTMnetiQ96529

Expressioni

Gene expression databases

ExpressionAtlasiQ96529 baseline and differential
GenevisibleiQ96529 AT

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi3702.AT3G57610.1

Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi67 – 77Combined sources11
Helixi81 – 88Combined sources8
Helixi89 – 91Combined sources3
Beta strandi93 – 97Combined sources5
Beta strandi106 – 109Combined sources4
Beta strandi115 – 121Combined sources7
Helixi123 – 126Combined sources4
Beta strandi131 – 134Combined sources4
Helixi142 – 153Combined sources12
Turni154 – 156Combined sources3
Turni160 – 162Combined sources3
Beta strandi163 – 171Combined sources9
Helixi174 – 186Combined sources13
Helixi199 – 207Combined sources9
Helixi214 – 218Combined sources5
Turni220 – 222Combined sources3
Helixi223 – 237Combined sources15
Helixi245 – 262Combined sources18
Turni263 – 265Combined sources3
Helixi269 – 278Combined sources10
Beta strandi283 – 290Combined sources8
Helixi291 – 293Combined sources3
Turni295 – 297Combined sources3
Helixi311 – 315Combined sources5
Turni321 – 323Combined sources3
Beta strandi327 – 341Combined sources15
Helixi350 – 359Combined sources10
Turni364 – 366Combined sources3
Beta strandi371 – 376Combined sources6
Helixi377 – 387Combined sources11
Beta strandi390 – 395Combined sources6
Helixi397 – 402Combined sources6
Beta strandi404 – 413Combined sources10
Beta strandi415 – 417Combined sources3
Helixi427 – 432Combined sources6
Beta strandi434 – 441Combined sources8
Helixi458 – 471Combined sources14
Beta strandi475 – 479Combined sources5
Beta strandi481 – 485Combined sources5
Beta strandi487 – 489Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DJ2X-ray2.90A/B48-490[»]
ProteinModelPortaliQ96529
SMRiQ96529
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96529

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni78 – 81IMP bindingUniRule annotation4
Regioni103 – 106IMP bindingUniRule annotation4
Regioni364 – 370Substrate bindingUniRule annotation7

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1355 Eukaryota
COG0104 LUCA
HOGENOMiHOG000260959
InParanoidiQ96529
KOiK01939
OMAiSNAGHTV
OrthoDBiEOG0936092X
PhylomeDBiQ96529

Family and domain databases

CDDicd03108 AdSS, 1 hit
HAMAPiMF_00011 Adenylosucc_synth, 1 hit
InterProiView protein in InterPro
IPR018220 Adenylosuccin_syn_GTP-bd
IPR033128 Adenylosuccin_syn_Lys_AS
IPR001114 Adenylosuccinate_synthetase
IPR027417 P-loop_NTPase
PANTHERiPTHR11846 PTHR11846, 1 hit
PfamiView protein in Pfam
PF00709 Adenylsucc_synt, 1 hit
SMARTiView protein in SMART
SM00788 Adenylsucc_synt, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00184 purA, 1 hit
PROSITEiView protein in PROSITE
PS01266 ADENYLOSUCCIN_SYN_1, 1 hit
PS00513 ADENYLOSUCCIN_SYN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96529-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSSLTLDS NPRFAVGGPY HRRYPPLHHP RSFVSCSAKR PAVSASLSVA
60 70 80 90 100
ADSAATESLG RIGSLSQVSG VLGCQWGDEG KGKLVDILAQ HFDIVARCQG
110 120 130 140 150
GANAGHTIYN SEGKKFALHL VPSGILNEDT TCVIGNGVVV HLPGLFKEID
160 170 180 190 200
GLESNGVSCK GRILVSDRAH LLFDFHQEVD GLRESELAKS FIGTTKRGIG
210 220 230 240 250
PAYSSKVIRN GIRVGDLRHM DTLPQKLDLL LSDAAARFQG FKYTPEMLRE
260 270 280 290 300
EVEAYKRYAD RLEPYITDTV HFINDSISQK KKVLVEGGQA TMLDIDFGTY
310 320 330 340 350
PFVTSSSPSA GGICTGLGIA PSVVGDLIGV VKAYTTRVGS GPFPTENLGT
360 370 380 390 400
GGDLLRLAGQ EFGTTTGRPR RCGWLDIVAL KFSCQINGFA SLNLTKLDVL
410 420 430 440 450
SDLNEIQLGV AYKRSDGTPV KSFPGDLRLL EELHVEYEVL PGWKSDISSV
460 470 480 490
RNYSDLPKAA QQYVERIEEL VGVPIHYIGI GPGRDALIYK
Length:490
Mass (Da):52,964
Last modified:February 1, 1997 - v1
Checksum:iB1E82BA386DF93CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49389 mRNA Translation: AAB16828.1
AL049660 Genomic DNA Translation: CAB41194.1
CP002686 Genomic DNA Translation: AEE79678.1
AY054606 mRNA Translation: AAK96797.1
AY081461 mRNA Translation: AAM10023.1
PIRiT06759
RefSeqiNP_191320.1, NM_115621.5
UniGeneiAt.22505

Genome annotation databases

EnsemblPlantsiAT3G57610.1; AT3G57610.1; AT3G57610
GeneIDi824930
GrameneiAT3G57610.1; AT3G57610.1; AT3G57610
KEGGiath:AT3G57610

Similar proteinsi

Entry informationi

Entry nameiPURA_ARATH
AccessioniPrimary (citable) accession number: Q96529
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 25, 2018
This is version 153 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

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health