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P28650 (PURA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.4

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit.

Enzyme regulation

Weakly inhibited by AMP non-competitively to all substrates. Inhibited by IMP non-competitively with respect to GTP. Inhibited by fructose 1,6-bisphosphate competitively with respect to IMP.

Pathway

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Note: Partially associated with particulate fractions.

Tissue specificity

High levels in muscle.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=12 µM for GTP Ref.4

KM=45 µM for IMP

KM=140 µM for L-aspartate

pH dependence:

Optimum pH is 6.6-6.9.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28650-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P28650-2)

The sequence of this isoform differs from the canonical sequence as follows:
     136-136: L → LENEVPHEPLPSASLLPMCWLLAP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Adenylosuccinate synthetase isozyme 1
PRO_0000095133

Regions

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

Sites

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

Amino acid modifications

Modified residue3881Phosphotyrosine By similarity

Natural variations

Alternative sequence1361L → LENEVPHEPLPSASLLPMCW LLAP in isoform 2.
VSP_008422

Secondary structure

1 .............................................................................. 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: EBEC85BF907B7FED

FASTA45750,254
        10         20         30         40         50         60 
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV 

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

       130        140        150        160        170        180 
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL 

       190        200        210        220        230        240 
RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY 

       250        260        270        280        290        300 
EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA 

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

       370        380        390        400        410        420 
LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE 

       430        440        450 
DLPPQAQSYV RFVENHMGVA VKWVGVGKSR ESMIQLF

« Hide

Isoform 2 [UniParc].

Checksum: 875588460688208D
Show »

FASTA48052,780

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a mouse muscle cDNA encoding adenylosuccinate synthetase."
Guicherit O.M., Rudolph F.B., Kellems R.E., Cooper B.F.
J. Biol. Chem. 266:22582-22587(1991) [PubMed: 1939273] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[2]"Amplification of an adenylosuccinate synthetase gene in alanosine-resistant murine T-lymphoma cells. Molecular cloning of a cDNA encoding the 'non-muscle' isozyme."
Guicherit O.M., Cooper B.F., Rudolph F.B., Kellems R.E.
J. Biol. Chem. 269:4488-4496(1994) [PubMed: 8308018] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Czech II.
Tissue: Mammary tumor.
[4]"Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance."
Borza T., Iancu C.V., Pike E., Honzatko R.B., Fromm H.J.
J. Biol. Chem. 278:6673-6679(2003) [PubMed: 12482871] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure."
Iancu C.V., Borza T., Choe J.Y., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 276:42146-42152(2001) [PubMed: 11560929] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
[6]"IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase."
Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 277:26779-26787(2002) [PubMed: 12004071] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IMP AND GTP.
[7]"Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase."
Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.
J. Biol. Chem. 277:40536-40543(2002) [PubMed: 12186864] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
[8]"Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases."
Iancu C.V., Zhou Y., Borza T., Fromm H.J., Honzatko R.B.
Biochemistry 45:11703-11711(2006) [PubMed: 16981730] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M74495 mRNA. Translation: AAA82870.1.
BC039943 mRNA. Translation: AAH39943.1.
IPIIPI00123190.
IPI00229690.
PIRAJMSDS. A39317.
RefSeqNP_031447.1. NM_007421.2.
UniGeneMm.3440.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IWEX-ray2.10A/B1-457[»]
1J4BX-ray2.50A1-457[»]
1LNYX-ray2.20A/B1-457[»]
1LONX-ray2.10A1-457[»]
1LOOX-ray2.20A1-457[»]
1MEZX-ray2.40A1-457[»]
1MF0X-ray2.50A1-457[»]
1MF1X-ray2.70A1-457[»]
2DGNX-ray2.40A1-457[»]
ProteinModelPortalP28650.
SMRP28650. Positions 27-457.
ModBaseSearch...

Protein-protein interaction databases

STRINGP28650.

PTM databases

PhosphoSiteP28650.

Proteomic databases

PRIDEP28650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021726; ENSMUSP00000021726; ENSMUSG00000011148.
GeneID11565.
KEGGmmu:11565.
UCSCuc011yvf.1. mouse.

Organism-specific databases

CTD122622.
MGIMGI:87947. Adssl1.

Phylogenomic databases

eggNOGroNOG05223.
GeneTreeENSGT00390000015553.
HOVERGENHBG053768.
OrthoDBEOG4P5K90.
PhylomeDBP28650.

Gene expression databases

ArrayExpressP28650.
BgeeP28650.
CleanExMM_ADSSL1.
GenevestigatorP28650.
GermOnlineENSMUSG00000011148. Mus musculus.

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...

Other

DrugBankDB00131. Adenosine monophosphate.
NextBio279066.
SOURCESearch...

Entry information

Entry namePURA1_MOUSE
AccessionPrimary (citable) accession number: P28650
Secondary accession number(s): Q8CHQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: November 16, 2011
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents