Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P46664 (PURA2_MOUSE)

Last modified November 3, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Hide | Top

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, non-muscle isozyme
    Adenylosuccinate synthetase, acidic isozyme
    IMP--aspartate ligase 2
Gene names
Name: Adss
Synonyms: Adss2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Enzyme regulation

Inhibited competitively by AMP and IMP and non-competitively by fructose 1,6-bisphosphate.

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the adenylosuccinate synthetase family.

Biophysicochemical properties

Kinetic parameters:

KM=15 µM for GTP

KM=12 µM for IMP

KM=950 µM for L-aspartate

pH dependence:

Optimum pH is 6.6-6.9.

Hide | Top

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological processAMP biosynthetic process Ref.1

Inferred from direct assay. Source: MGI

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity Ref.1 Ref.2

Inferred from direct assay. Source: MGI

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Adenylosuccinate synthetase isozyme 2
PRO_0000095131

Regions

Nucleotide binding39 – 457GTP Potential

Sites

Active site1731 By similarity
Active site1801 By similarity
Metal binding401Magnesium By similarity
Metal binding671Magnesium; via carbonyl oxygen By similarity

Experimental info

Sequence conflict1671G → R in AAA19727. Ref.1
Sequence conflict1991A → T in AAA19727. Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P46664-1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 7825B758BC6CDA38

FASTA45650,021
        10         20         30         40         50         60 
MSISESSPAA TSLPNGDCGR PRARSGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC 

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

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

       190        200        210        220        230        240 
MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQQL KGYMERIKPM VKDGVYFLYE 

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

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

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

       430        440        450 
LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/Sv.
Tissue: Kidney.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Cerebellum and Liver.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

L24554 mRNA. Translation: AAA19727.1.
AK004877 mRNA. Translation: BAB23635.1.
AK010263 mRNA. Translation: BAB26805.1.
AK028060 mRNA. Translation: BAC25730.1.
AK148420 mRNA. Translation: BAE28543.1.
AK170279 mRNA. Translation: BAE41682.1.
IPIIPI00135969.
PIRA53162.
RefSeqNP_031448.2.
UniGeneMm.338021

3D structure databases

HSSPHSSP built from PDB template 1IWE based on UniProtKB P28650.
SMRP46664. Positions 27-456.
ModBaseSearch...

Protein-protein interaction databases

STRINGP46664.

PTM databases

PhosphoSiteP46664.

2-D gel databases

REPRODUCTION-2DPAGEP46664.

Proteomic databases

PRIDEP46664.

Genome annotation databases

EnsemblENSMUST00000016105; ENSMUSP00000016105; ENSMUSG00000015961; Mus musculus. [Genome view]
GeneID11566.
KEGGmmu:11566.
UCSCuc007dut.1. mouse.

Organism-specific databases

CTD11566.
MGIMGI:87948. Adss.

Phylogenomic databases

HOGENOMP46664.
HOVERGENP46664.
OMAQYKSMYP.

Enzyme and pathway databases

BRENDA6.3.4.4. 244.

Gene expression databases

ArrayExpressP46664.
BgeeP46664.
CleanExMM_ADSS.
GenevestigatorP46664.
GermOnlineENSMUSG00000015961. Mus musculus.

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]
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 Resources

NextBio279070.
SOURCESearch...

Hide | Top

Entry information

Entry namePURA2_MOUSE
AccessionPrimary (citable) accession number: P46664
Secondary accession number(s): Q9CQL9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 7, 2006
Last modified: November 3, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

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

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