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A4Z6H0 (PURA1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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):
Adenylosuccinate synthetase, basic isozyme
Adenylosuccinate synthetase, muscle isozyme
Short name=M-type adenylosuccinate synthetase
IMP--aspartate ligase 1
Gene names
Name:ADSSL1
Synonyms:ADSS1
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP 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.

Tissue specificity

Predominantly expressed in the striated muscle tissues. Ref.1

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
   Technical termComplete proteome
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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Adenylosuccinate synthetase isozyme 1
PRO_0000321961

Regions

Nucleotide binding42 – 487GTP By similarity
Nucleotide binding70 – 723GTP By similarity
Nucleotide binding363 – 3653GTP By similarity
Nucleotide binding445 – 4484GTP By similarity
Region43 – 464IMP binding By similarity
Region68 – 714IMP binding By similarity
Region331 – 3377Substrate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site711Proton donor By similarity
Metal binding431Magnesium By similarity
Metal binding701Magnesium; via carbonyl oxygen By similarity
Binding site431Substrate By similarity
Binding site1631IMP By similarity
Binding site1771IMP; shared with dimeric partner By similarity
Binding site2561IMP By similarity
Binding site2711IMP By similarity
Binding site3351IMP By similarity
Binding site3371GTP By similarity

Amino acid modifications

Modified residue3881Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4Z6H0 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: CF4DFDAEE379BC66

FASTA45750,098
        10         20         30         40         50         60 
MSGTRASNDR PPSAGGVKRG RLQHEAATTG SRVTVVLGAQ WGDEGKGKVV DLLATDADII 

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

       130        140        150        160        170        180 
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTRKGIGPA YSSKAARAGL 

       190        200        210        220        230        240 
RVCDLLSDFD EFSARFRNLA RQHQSMFPTL ETDVEGQLKK LKGFAERIRP MVRDGVYFMY 

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

       310        320        330        340        350        360 
YTTRVGVGAF PTEQINETGD LLQSRGHEWG VTTGRKRRCG WLDLMILRYA HMINGFTALA 

       370        380        390        400        410        420 
LTKLDILDTL DEVKVGVSYK LSGKRIPYFP ANQEILQKVE VEYETLPGWK TDTTGARKWE 

       430        440        450 
DLPPQAQSYI RFVENHVGVA VKWVGVGKSR DSMIQLF

« Hide

References

[1]"Comparative molecular characterization of ADSS1 and ADSS2 genes in pig (Sus scrofa)."
Li X., Zhu Z., Mo D., Wang H., Yang S., Zhao S., Li K.
Comp. Biochem. Physiol. 147B:271-277(2007) [PubMed: 17347008] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ462751 mRNA. Translation: ABE73154.1.
RefSeqNP_001090978.1. NM_001097509.1.
UniGeneSsc.24153.

3D structure databases

ProteinModelPortalA4Z6H0.
SMRA4Z6H0. Positions 29-457.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100048943.
KEGGssc:100048943.

Organism-specific databases

CTD122622.

Phylogenomic databases

HOVERGENHBG053768.

Enzyme and pathway databases

BRENDA6.3.4.4. 6170.

Family and domain databases

InterProIPR018220. Adenylosuccinate_synthase_AS.
IPR001114. Adenylosuccinate_synthetase.
[Graphical view]
KOK01939.
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...

Entry information

Entry namePURA1_PIG
AccessionPrimary (citable) accession number: A4Z6H0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: November 16, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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