Reviewed, UniProtKB/Swiss-Prot P46664 (PURA2_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Gene Ontology (GO)
Biological process	AMP biosynthetic process Ref.1 Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 456	456	Adenylosuccinate synthetase isozyme 2		PRO_0000095131
Regions
	Nucleotide binding	39 – 45	7	GTP Potential
Sites
	Active site	173	1	By similarity
	Active site	180	1	By similarity
	Metal binding	40	1	Magnesium By similarity
	Metal binding	67	1	Magnesium; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	167	1	G → R in AAA19727. Ref.1
	Sequence conflict	199	1	A → T in AAA19727. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P46664-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 7825B758BC6CDA38	FASTA	456	50,021
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00135969.
PIR	A53162.
RefSeq	NP_031448.2.
UniGene	Mm.338021
3D structure databases
SMR	P46664. Positions 26-456.
ModBase	Search...
Protein-protein interaction databases
STRING	P46664.
PTM databases
PhosphoSite	P46664.
2-D gel databases
REPRODUCTION-2DPAGE	P46664.
Proteomic databases
PRIDE	P46664.
Genome annotation databases
Ensembl	ENSMUST00000016105; ENSMUSP00000016105; ENSMUSG00000015961; Mus musculus. [Genome view]
GeneID	11566.
KEGG	mmu:11566.
UCSC	uc007dut.1. mouse.
Organism-specific databases
CTD	11566.
MGI	MGI:87948. Adss.
Phylogenomic databases
eggNOG	roNOG05223.
HOGENOM	HBG658237.
HOVERGEN	P46664.
InParanoid	P46664.
OMA	PIHRAID.
OrthoDB	EOG9X3KKW.
PhylomeDB	P46664.
Enzyme and pathway databases
BRENDA	6.3.4.4. 244.
Gene expression databases
ArrayExpress	P46664.
Bgee	P46664.
CleanEx	MM_ADSS.
Genevestigator	P46664.
GermOnline	ENSMUSG00000015961. Mus musculus.
Family and domain databases
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
SMART	SM00788. Adenylsucc_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR00184. purA. 1 hit.
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279070.
SOURCE	Search...

Entry information

Entry name

PURA2_MOUSE

Accession

Primary (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:	February 9, 2010
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)