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P46664 (PURA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
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 length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.2

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 Ref.2

KM=12 µM for IMP

KM=950 µM for L-aspartate

pH dependence:

Optimum pH is 6.6-6.9.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processAMP biosynthetic process

Inferred from direct assay Ref.1. Source: MGI

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylosuccinate synthase activity

Inferred from direct assay Ref.2Ref.1. Source: MGI

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Adenylosuccinate synthetase isozyme 2
PRO_0000095131

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

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
P46664 [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

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], FUNCTION, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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. NM_007422.3.
UniGeneMm.338021.

3D structure databases

ProteinModelPortalP46664.
SMRP46664. Positions 26-456.
ModBaseSearch...

Protein-protein interaction databases

STRINGP46664.

PTM databases

PhosphoSiteP46664.

2D gel databases

REPRODUCTION-2DPAGEP46664.
Q9CQL9.

Proteomic databases

PRIDEP46664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016105; ENSMUSP00000016105; ENSMUSG00000015961.
GeneID11566.
KEGGmmu:11566.

Organism-specific databases

CTD159.
MGIMGI:87948. Adss.

Phylogenomic databases

eggNOGroNOG05223.
HOGENOMHBG658237.
HOVERGENHBG053768.
InParanoidP46664.
OMAPIHRAID.
OrthoDBEOG4P5K90.
PhylomeDBP46664.

Gene expression databases

ArrayExpressP46664.
BgeeP46664.
CleanExMM_ADSS.
GenevestigatorP46664.
GermOnlineENSMUSG00000015961. 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

NextBio279070.
SOURCESearch...

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 16, 2011
This is version 104 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

SIMILARITY comments

Index of protein domains and families

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