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Protein

Adenylosuccinate synthetase, chloroplastic

Gene

PURA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 + N(6)-(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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

GTP-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

TAIRiAT3G57610.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • plastid Source: TAIR
Complete GO annotation...

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

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.
OMAiFHHAKPI.
OrthoDBiEOG0936092X.
PhylomeDBiQ96529.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11846. PTHR11846. 1 hit.
PfamiPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTiSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00184. purA. 1 hit.
PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

STRINGi3702.AT3G57610.1.

PTM databases

iPTMnetiQ96529.

Proteomic databases

PaxDbiQ96529.
PRIDEiQ96529.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G57610.

Phylogenomic databases

eggNOGiKOG1355. Eukaryota.
COG0104. LUCA.
HOGENOMiHOG000260959.
InParanoidiQ96529.
KOiK01939.
OMAiFHHAKPI.
OrthoDBiEOG0936092X.
PhylomeDBiQ96529.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ96529.
PROiQ96529.

Gene expression databases

GenevisibleiQ96529. AT.

Family and domain databases

CDDicd03108. AdSS. 1 hit.
HAMAPiMF_00011. Adenylosucc_synth. 1 hit.
InterProiIPR018220. Adenylosuccin_syn_GTP-bd.
IPR033128. Adenylosuccin_syn_Lys_AS.
IPR001114. Adenylosuccinate_synthetase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11846. PTHR11846. 1 hit.
PfamiPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTiSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00184. purA. 1 hit.
PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPURA_ARATH
AccessioniPrimary (citable) accession number: Q96529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 30, 2016
This is version 147 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.