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A4Z6H1 (PURA2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 40. 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 2
Short name=AMPSase 2
Short name=AdSS 2
EC=6.3.4.4
Alternative name(s):
Adenylosuccinate synthetase, acidic isozyme
Adenylosuccinate synthetase, liver isozyme
Short name=L-type adenylosuccinate synthetase
IMP--aspartate ligase 2
Gene names
Name:ADSS
Synonyms:ADSS2
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 length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   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

Initiator methionine11Removed By similarity
Chain2 – 456455Adenylosuccinate synthetase isozyme 2
PRO_0000321959

Regions

Nucleotide binding39 – 457GTP Potential
Nucleotide binding67 – 693GTP
Nucleotide binding362 – 3643GTP
Nucleotide binding444 – 4474GTP
Region40 – 434IMP binding By similarity
Region65 – 684IMP binding By similarity
Region330 – 3367Substrate binding By similarity

Sites

Active site401Proton acceptor By similarity
Active site681Proton donor By similarity
Metal binding401Magnesium By similarity
Metal binding671Magnesium; via carbonyl oxygen By similarity
Binding site401Substrate By similarity
Binding site1621IMP By similarity
Binding site1761IMP; shared with dimeric partner By similarity
Binding site2551IMP By similarity
Binding site2701IMP By similarity
Binding site3341IMP By similarity
Binding site3361GTP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4Z6H1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 1BB046D2ADB80A6C

FASTA45650,140
        10         20         30         40         50         60 
MAFAETNPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC 

        70         80         90        100        110        120 
QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL 

       130        140        150        160        170        180 
EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR 

       190        200        210        220        230        240 
MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQKL KGYMERIKPM VRDGVYFLYE 

       250        260        270        280        290        300 
ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 

       310        320        330        340        350        360 
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL 

       370        380        390        400        410        420 
TKLDILDMFT EIKVGVAYKL DGEIIPHFPA NQEVLNKVEV QYKTLPGWNT DISNARTFKE 

       430        440        450 
LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF

« 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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ463129 mRNA. Translation: ABE73156.1.
RefSeqNP_001090977.1. NM_001097508.1.
UniGeneSsc.32636.

3D structure databases

ProteinModelPortalA4Z6H1.
SMRA4Z6H1. Positions 26-456.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4Z6H1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100048942.
KEGGssc:100048942.

Organism-specific databases

CTD159.

Phylogenomic databases

GeneTreeENSGT00390000015553.
HOVERGENHBG053768.
OrthoDBEOG4P5K90.

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 namePURA2_PIG
AccessionPrimary (citable) accession number: A4Z6H1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: November 16, 2011
This is version 40 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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