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Reviewed, UniProtKB/Swiss-Prot A5G293 (PURA_ACICJ)

Last modified November 3, 2009. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Adenylosuccinate synthetase
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase
    AdSS
    AMPSase
Gene names
Name: purA
Ordered Locus Names: Acry_2784
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Plays an important role in the de novo pathway of purine nucleotide biosynthesis. HAMAP MF_00011

Catalytic activity

GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP MF_00011

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: HAMAP

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Adenylosuccinate synthetase HAMAP MF_00011
PRO_1000000769

Regions

Nucleotide binding12 – 187GTP Potential

Sites

Active site1401 By similarity
Active site1471 By similarity
Metal binding131Magnesium By similarity
Metal binding401Magnesium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5G293-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: EE1D5D5B8BA11653

FASTA42945,483
        10         20         30         40         50         60 
MANVTIIGAQ WGDEGKGKVV DWLASRADVV VRFQGGHNAG HTLVVGNQTY KLSLLPSGLV 

        70         80         90        100        110        120 
RGKLGVIGNG VVVDPVALLA EIGRVREQGL NVTPETLRIA DNAPLILPLH AALDAAREAA 

       130        140        150        160        170        180 
RGARRIGTTG RGIGPAYEDK VARRAIRICD LAEPETLDWR LDELLLHHNT LLAGLGAPTF 

       190        200        210        220        230        240 
GKAELMDQLL ALAPQILPFA EPVWERLAEA KKSGARILFE GAQAVMLDVD HGTYPFVTSS 

       250        260        270        280        290        300 
NTVSGQIAAG AGVGPDAAGR VLGIAKAYST RVGSGPFPTE QDNETGRLLG ERGHEFGTVT 

       310        320        330        340        350        360 
GRARRCGWFD AALVRQAVKV GGIQGLALTK LDVLDGMTTL QIGVGYRIGG ETLPHLPPGA 

       370        380        390        400        410        420 
AAQAKAEPVY ETIEGWSGST RGARSYADLP AQAIKYVRRI EELVECPVTL LSTSPERDDT 


ILMQDPFAD 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000697 Genomic DNA. Translation: ABQ31975.1.
RefSeqYP_001235894.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5G293.

Genome annotation databases

GeneID5159997.
GenomeReviewsGene locus Acry_2784 in contig CP000697_GR.
KEGGacr:Acry_2784.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIPVCVAY.

Family and domain databases

HAMAPMF_00011.
[Tree]
InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[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...

Entry information

Entry namePURA_ACICJ
AccessionPrimary (citable) accession number: A5G293
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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