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Reviewed, UniProtKB/Swiss-Prot Q96529 (PURA_ARATH)

Last modified February 9, 2010. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase, chloroplastic
      Short name=AMPSase
      Short name=AdSS
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
Gene names
Ordered Locus Names: At3g57610
ORF Names: F15B8.200
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis.

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.

Subunit structure

Homodimer.

Subcellular location

Plastid › chloroplast.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast
Chain? – 490Adenylosuccinate synthetase, chloroplasticPRO_0000029870

Regions

Nucleotide binding77 – 837GTP Potential

Sites

Active site2061 By similarity
Active site2131 By similarity
Metal binding781Magnesium By similarity
Metal binding1051Magnesium; via carbonyl oxygen By similarity

Secondary structure

1 .......................................................................... 490
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q96529-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B1E82BA386DF93CB

FASTA49052,964
        10         20         30         40         50         60 
MSLSSLTLDS NPRFAVGGPY HRRYPPLHHP RSFVSCSAKR PAVSASLSVA ADSAATESLG 

        70         80         90        100        110        120 
RIGSLSQVSG VLGCQWGDEG KGKLVDILAQ HFDIVARCQG GANAGHTIYN SEGKKFALHL 

       130        140        150        160        170        180 
VPSGILNEDT TCVIGNGVVV HLPGLFKEID GLESNGVSCK GRILVSDRAH LLFDFHQEVD 

       190        200        210        220        230        240 
GLRESELAKS FIGTTKRGIG PAYSSKVIRN GIRVGDLRHM DTLPQKLDLL LSDAAARFQG 

       250        260        270        280        290        300 
FKYTPEMLRE EVEAYKRYAD RLEPYITDTV HFINDSISQK KKVLVEGGQA TMLDIDFGTY 

       310        320        330        340        350        360 
PFVTSSSPSA GGICTGLGIA PSVVGDLIGV VKAYTTRVGS GPFPTENLGT GGDLLRLAGQ 

       370        380        390        400        410        420 
EFGTTTGRPR RCGWLDIVAL KFSCQINGFA SLNLTKLDVL SDLNEIQLGV AYKRSDGTPV 

       430        440        450        460        470        480 
KSFPGDLRLL EELHVEYEVL PGWKSDISSV RNYSDLPKAA QQYVERIEEL VGVPIHYIGI 

       490 
GPGRDALIYK

« Hide

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References

« Hide 'large scale' references
[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: 8790347] [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. expand/collapse author list , 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: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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: 10669609] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 48-490.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U49389 mRNA. Translation: AAB16828.1.
AL049660 Genomic DNA. Translation: CAB41194.1.
AY054606 mRNA. Translation: AAK96797.1.
AY081461 mRNA. Translation: AAM10023.1.
IPIIPI00516677.
PIRT06759.
RefSeqNP_191320.1.
UniGeneAt.22505
Rra.190
Rsa.11088
Rsa.22205

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ2X-ray2.90A/B48-490[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96529.

Proteomic databases

PRIDEQ96529.
ProMEXQ96529.

Genome annotation databases

GeneID824930.
GenomeReviewsGene locus AT3G57610 in contig BA000014_GR.
KEGGath:AT3G57610.
NMPDRfig|3702.1.peg.17097.

Organism-specific databases

TAIRAt3g57610.

Phylogenomic databases

HOGENOMHBG658237.
InParanoidQ96529.
OMAKRGRLQQ.
PhylomeDBQ96529.

Enzyme and pathway databases

BRENDA6.3.4.4. 302.

Gene expression databases

ArrayExpressQ96529.
GenevestigatorQ96529.
GermOnlineAT3G57610. Arabidopsis thaliana.

Family and domain databases

InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
SMARTSM00788. Adenylsucc_synt. 1 hit.
[Graphical view]
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePURA_ARATH
AccessionPrimary (citable) accession number: Q96529
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 9, 2010
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents