Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O24396 (PURA_WHEAT)

Last modified December 16, 2008. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Hide | Top

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
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Hide | Top

Protein attributes

Sequence length476 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords

   Biological processPurine biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionGTP binding

Inferred from electronic annotation. Source: InterPro

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – ?Chloroplast
Chain? – 476Adenylosuccinate synthetase, chloroplasticPRO_0000029872

Regions

Nucleotide binding63 – 697GTP Potential

Sites

Active site1921 By similarity
Active site1991 By similarity
Metal binding641Magnesium By similarity
Metal binding911Magnesium; via carbonyl oxygen By similarity

Experimental info

Non-terminal residue11

Secondary structure

1 ................................................................................... 476
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O24396-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7E2D9E7F616783DF

FASTA47650,918
        10         20         30         40         50         60 
AAAAAGRGRS FSPAAPAPSS VRLPGRQAPA PAAASALAVE ADPAADRVSS LSQVSGVLGS 

        70         80         90        100        110        120 
QWGDEGKGKL VDVLAPRFDI VARCQGGANA GHTIYNSEGK KFALHLVPSG ILHEGTLCVV 

       130        140        150        160        170        180 
GNGAVIHVPG FFGEIDGLQS NGVSCDGRIL VSDRAHLLFD LHQTVDGLRE AELANSFIGT 

       190        200        210        220        230        240 
TKRGIGPCYS SKVTRNGLRV CDLRHMDTFG DKLDVLFEDA AARFEGFKYS KGMLKEEVER 

       250        260        270        280        290        300 
YKRFAERLEP FIADTVHVLN ESIRQKKKIL VEGGQATMLD IDFGTYPFVT SSSPSAGGIC 

       310        320        330        340        350        360 
TGLGIAPRVI GDLIGVVKAY TTRVGSGPFP TELLGEEGDV LRKAGMEFGT TTGRPRRCGW 

       370        380        390        400        410        420 
LDIVALKYCC DINGFSSLNL TKLDVLSGLP EIKLGVSYNQ MDGEKLQSFP GDLDTLEQVQ 

       430        440        450        460        470 
VNYEVLPGWD SDISSVRSYS ELPQAARRYV ERIEELAGVP VHYIGVGPGR DALIYK

« Hide

Hide | Top

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].
Strain: cv. Kanzler.
[2]"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 (3.0 ANGSTROMS) OF 35-476.

Hide | Top

Cross-references

Sequence databases

U49387 mRNA. Translation: AAB16829.1.
PIRT06792.
UniGeneTa.121

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DJ3X-ray3.00A/B35-476[»]
ModBaseSearch...

Organism-specific databases

GrameneO24396.

Family and domain databases

InterProIPR001114. AdlSucc_Synth.
[Graphical view]
PANTHERPTHR11846. Asucc_synthtase. 1 hit.
PfamPF00709. Adenylsucc_synt. 1 hit.
[Graphical view]
ProDomPD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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...

Hide | Top

Entry information

Entry namePURA_WHEAT
AccessionPrimary (citable) accession number: O24396
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: December 16, 2008
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

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