Reviewed, UniProtKB/Swiss-Prot P28650 (PURA1_MOUSE)

Names and origin

Protein names

Recommended name:
    Adenylosuccinate synthetase isozyme 1
      Short name=AMPSase 1
      Short name=AdSS 1
    EC=6.3.4.4
Alternative name(s):
    Adenylosuccinate synthetase, muscle isozyme
    IMP--aspartate ligase 1

Gene names

Name:	Adssl1
Synonyms:	Adss1

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	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.

Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.1 Inferred from direct assay. Source: MGI extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylosuccinate synthase activity Ref.1 Inferred from direct assay. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

Adenylosuccinate synthetase isozyme 1

PRO_0000095133

Regions

Nucleotide binding

42 – 48

7

GTP Potential

Sites

Active site

174

1

By similarity

Active site

181

1

By similarity

Metal binding

43

1

Magnesium

Metal binding

70

1

Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue

388

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

136

1

L → LENEVPHEPLPSASLLPMCW LLAP in isoform 2.

VSP_008422

Secondary structure

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457

Helix Strand Turn

Details...

Beta strand

33 – 42

10

Helix

46 – 54

9

Beta strand

58 – 62

5

Beta strand

71 – 74

4

Beta strand

79 – 85

7

Helix

87 – 90

4

Beta strand

94 – 98

5

Beta strand

102 – 104

3

Helix

106 – 117

12

Turn

118 – 120

3

Helix

124 – 126

3

Beta strand

127 – 131

5

Helix

139 – 155

17

Beta strand

164 – 166

3

Helix

167 – 175

9

Helix

182 – 185

4

Helix

189 – 205

17

Helix

214 – 228

15

Helix

229 – 231

3

Helix

235 – 244

10

Beta strand

250 – 253

4

Helix

258 – 260

3

Turn

262 – 264

3

Helix

278 – 284

7

Helix

288 – 290

3

Beta strand

291 – 304

14

Beta strand

306 – 308

3

Helix

317 – 325

9

Turn

331 – 333

3

Beta strand

338 – 340

3

Helix

344 – 354

11

Beta strand

357 – 362

6

Helix

364 – 367

4

Beta strand

371 – 381

11

Helix

395 – 398

4

Beta strand

400 – 407

8

Helix

419 – 421

3

Helix

424 – 437

14

Beta strand

441 – 445

5

Beta strand

447 – 449

3

Turn

450 – 452

3

Beta strand

453 – 455

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: EBEC85BF907B7FED	FASTA	457	50,254
	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
	Isoform 2. Checksum: 875588460688208D	FASTA	480	52,780
	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 SDRAHLENEV PHEPLPSASL LPMCWLLAPV FDFHQAVDGL QEVQRQAQEG 190 200 210 220 230 240 KNIGTTKKGI GPTYSSKAAR TGLRICDLLS DFDEFSARFK NLAHQHQSMF PTLEIDVEGQ 250 260 270 280 290 300 LKRLKGFAER IRPMVRDGVY FMYEALHGPP KKVLVEGANA ALLDIDFGTY PFVTSSNCTV 310 320 330 340 350 360 GGVCTGLGIP PQNIGDVYGV VKAYTTRVGI GAFPTEQINE IGDLLQNRGH EWGVTTGRKR 370 380 390 400 410 420 RCGWLDLMIL RYAHMVNGFT ALALTKLDIL DVLSEIKVGI SYKLNGKRIP YFPANQEILQ 430 440 450 460 470 480 KVEVEYETLP GWKADTTGAR KWEDLPPQAQ SYVRFVENHM GVAVKWVGVG KSRESMIQLF

References

	« Hide 'large scale' referencesShow '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]	"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 (2.4 ANGSTROMS).
[5]	"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 (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M74495 mRNA. Translation: AAA82870.1.
BC039943 mRNA. Translation: AAH39943.1.

IPI

IPI00123190.
IPI00229690.

PIR

AJMSDS. A39317.

RefSeq

NP_031447.1.

UniGene

Mm.3440

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IWE	X-ray	2.10	A/B	1-457	[»]
1J4B	X-ray	2.50	A	1-457	[»]
1LNY	X-ray	2.20	A/B	1-457	[»]
1LON	X-ray	2.10	A	1-457	[»]
1LOO	X-ray	2.20	A	1-457	[»]
1MEZ	X-ray	2.40	A	1-457	[»]
1MF0	X-ray	2.50	A	1-457	[»]
1MF1	X-ray	2.70	A	1-457	[»]
2DGN	X-ray	2.40	A	1-457	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P28650.

PTM databases

PhosphoSite

P28650.

Proteomic databases

PRIDE

P28650.

Genome annotation databases

Ensembl

ENSMUST00000021726; ENSMUSP00000021726; ENSMUSG00000011148; Mus musculus. [Genome view]
ENSMUST00000109756; ENSMUSP00000105378; ENSMUSG00000011148; Mus musculus. [Genome view]

GeneID

11565.

KEGG

mmu:11565.

UCSC

uc007peu.1. mouse.

Organism-specific databases

CTD

11565.

MGI

MGI:87947. Adssl1.

Phylogenomic databases

HOGENOM

P28650.

HOVERGEN

P28650.

Enzyme and pathway databases

BRENDA

6.3.4.4. 244.

Gene expression databases

ArrayExpress

P28650.

Bgee

P28650.

CleanEx

MM_ADSSL1.

Genevestigator

P28650.

GermOnline

ENSMUSG00000011148. 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]

ProDom

PD001188. Asucc_synthtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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

DrugBank

DB00131. Adenosine monophosphate.

NextBio

279066.

SOURCE

Search...

Entry information

Entry name

PURA1_MOUSE

Accession

Primary (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:	October 13, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)