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Reviewed, UniProtKB/Swiss-Prot A5PJR4 (PURA1_BOVIN)

Last modified September 1, 2009. Version 22. 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 isozyme 1
      Short name=AMPSase 1
      Short name=AdSS 1
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase 1
Gene names
Name: ADSSL1
Synonyms: ADSS1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

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 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
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processpurine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Adenylosuccinate synthetase isozyme 1
PRO_0000321960

Regions

Nucleotide binding42 – 487GTP Potential

Sites

Active site1741 By similarity
Active site1811 By similarity
Metal binding431Magnesium By similarity
Metal binding701Magnesium; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue3881Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5PJR4-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 202C6350F68068F5

FASTA45750,134
        10         20         30         40         50         60 
MSGTRASNDR PPSAGGVKRG RLQHEAATTG SRVTVVLGAQ WGDEGKGKVV DLLATDADVV 

        70         80         90        100        110        120 
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NPKAVSFIGN GVVVHLPGLF EEAEKNEKKG 

       130        140        150        160        170        180 
LKDWEKRLVI SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTRKGIGPA YSSKAARTGL 

       190        200        210        220        230        240 
RICDLLSDFD EFSSRFKNLA RQHQSMFPSL EVDVEGQLKR LKGFAERIRP MVRDGVYFMY 

       250        260        270        280        290        300 
EALHGPPKKI LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGEVYGVVKA 

       310        320        330        340        350        360 
YTTRVGIGAF PTEQINEIGD LLQSRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA 

       370        380        390        400        410        420 
LTKLDILDAL DEIKVGVAYK LGGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE 

       430        440        450 
DLPPQAQSYI RFVENHVGVA VKWVGVGKSR DSMIQLF 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal muscle.

Cross-references

Sequence databases

BC142211 mRNA. Translation: AAI42212.1.
IPIIPI00707722.
RefSeqNP_001092662.1.
UniGeneBt.16782

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5PJR4.

Genome annotation databases

EnsemblENSBTAT00000044296; ENSBTAP00000041803; ENSBTAG00000017616; Bos taurus. [Genome view]
GeneID784089.
KEGGbta:784089.

Organism-specific databases

CTD784089.

Enzyme and pathway databases

BRENDA6.3.4.4. 251.

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]
ProDomPD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00184. purA. 1 hit.
PROSITEPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURA1_BOVIN
AccessionPrimary (citable) accession number: A5PJR4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: September 1, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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