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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)
  2. Adenylosuccinate lyase (At1g36280), Adenylosuccinate lyase (At1g36280), Adenylosuccinate lyase (F15C21.8), 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei78 – 781Proton acceptorUniRule annotation
Metal bindingi78 – 781MagnesiumUniRule annotation
Metal bindingi105 – 1051Magnesium; via carbonyl oxygenUniRule annotation
Active sitei106 – 1061Proton donorUniRule annotation
Binding sitei195 – 1951IMPUniRule annotation
Binding sitei209 – 2091IMP; shared with dimeric partnerUniRule annotation
Binding sitei289 – 2891IMPUniRule annotation
Binding sitei304 – 3041IMPUniRule annotation
Binding sitei368 – 3681IMPUniRule annotation
Binding sitei370 – 3701GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 837GTP
Nucleotide bindingi105 – 1073GTP
Nucleotide bindingi396 – 3983GTP
Nucleotide bindingi479 – 4813GTP

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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545ChloroplastCombined sourcesAdd
BLAST
Chaini46 – 490445Adenylosuccinate synthetase, chloroplasticPRO_0000029870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N-acetylserineCombined sources

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

1
490
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 7711Combined sources
Helixi81 – 888Combined sources
Helixi89 – 913Combined sources
Beta strandi93 – 975Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi115 – 1217Combined sources
Helixi123 – 1264Combined sources
Beta strandi131 – 1344Combined sources
Helixi142 – 15312Combined sources
Turni154 – 1563Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1719Combined sources
Helixi174 – 18613Combined sources
Helixi199 – 2079Combined sources
Helixi214 – 2185Combined sources
Turni220 – 2223Combined sources
Helixi223 – 23715Combined sources
Helixi245 – 26218Combined sources
Turni263 – 2653Combined sources
Helixi269 – 27810Combined sources
Beta strandi283 – 2908Combined sources
Helixi291 – 2933Combined sources
Turni295 – 2973Combined sources
Helixi311 – 3155Combined sources
Turni321 – 3233Combined sources
Beta strandi327 – 34115Combined sources
Helixi350 – 35910Combined sources
Turni364 – 3663Combined sources
Beta strandi371 – 3766Combined sources
Helixi377 – 38711Combined sources
Beta strandi390 – 3956Combined sources
Helixi397 – 4026Combined sources
Beta strandi404 – 41310Combined sources
Beta strandi415 – 4173Combined sources
Helixi427 – 4326Combined sources
Beta strandi434 – 4418Combined sources
Helixi458 – 47114Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi481 – 4855Combined sources
Beta strandi487 – 4893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ2X-ray2.90A/B48-490[»]
ProteinModelPortaliQ96529.
SMRiQ96529. Positions 62-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96529.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni78 – 814IMP bindingUniRule annotation
Regioni103 – 1064IMP bindingUniRule annotation
Regioni364 – 3707Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the adenylosuccinate synthetase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

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

Family and domain databases

HAMAPiMF_00011. Adenylosucc_synth.
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_115621.4.
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_115621.4.
UniGeneiAt.22505.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ2X-ray2.90A/B48-490[»]
ProteinModelPortaliQ96529.
SMRiQ96529. Positions 62-490.
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.
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

HAMAPiMF_00011. Adenylosucc_synth.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The mode of action and the structure of a herbicide in complex with its target: binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase."
    Fonne-Pfister R., Chemla P., Ward E., Girardet M., Kreuz K.E., Honzatko R.B., Fromm H.J., Schaer H.-P., Gruetter M.G., Cowan-Jacob S.W.
    Proc. Natl. Acad. Sci. U.S.A. 93:9431-9436(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-46, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana."
    Prade L., Cowan-Jacob S.W., Chemla P., Potter S., Ward E., Fonne-Pfister R.
    J. Mol. Biol. 296:569-577(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 48-490 IN COMPLEX WITH GDP.

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: July 6, 2016
This is version 143 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.