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Adenylosuccinate synthetase isozyme 1 (AMPSase 1) (AdSS 1) (EC 6.3.4.4) (Adenylosuccinate synthetase, basic isozyme) (Adenylosuccinate synthetase, muscle isozyme) (M-type adenylosuccinate synthetase) (IMP--aspartate ligase 1)

 PURA1_MOUSE             Reviewed;         457 AA.
P28650; Q8CHQ1;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
20-JUN-2018, entry version 161.
RecName: Full=Adenylosuccinate synthetase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_03126};
Short=AMPSase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
Short=AdSS 1 {ECO:0000255|HAMAP-Rule:MF_03126};
EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03126};
AltName: Full=Adenylosuccinate synthetase, basic isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
AltName: Full=Adenylosuccinate synthetase, muscle isozyme {ECO:0000255|HAMAP-Rule:MF_03126};
Short=M-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03126};
AltName: Full=IMP--aspartate ligase 1 {ECO:0000255|HAMAP-Rule:MF_03126};
Name=Adssl1; Synonyms=Adss1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=1939273;
Guicherit O.M., Rudolph F.B., Kellems R.E., Cooper B.F.;
"Molecular cloning and expression of a mouse muscle cDNA encoding
adenylosuccinate synthetase.";
J. Biol. Chem. 266:22582-22587(1991).
[2]
SEQUENCE REVISION.
PubMed=8308018;
Guicherit O.M., Cooper B.F., Rudolph F.B., Kellems R.E.;
"Amplification of an adenylosuccinate synthetase gene in alanosine-
resistant murine T-lymphoma cells. Molecular cloning of a cDNA
encoding the 'non-muscle' isozyme.";
J. Biol. Chem. 269:4488-4496(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12482871; DOI=10.1074/jbc.M210838200;
Borza T., Iancu C.V., Pike E., Honzatko R.B., Fromm H.J.;
"Variations in the response of mouse isozymes of adenylosuccinate
synthetase to inhibitors of physiological relevance.";
J. Biol. Chem. 278:6673-6679(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
PubMed=11560929; DOI=10.1074/jbc.M106294200;
Iancu C.V., Borza T., Choe J.Y., Fromm H.J., Honzatko R.B.;
"Recombinant mouse muscle adenylosuccinate synthetase: overexpression,
kinetics, and crystal structure.";
J. Biol. Chem. 276:42146-42152(2001).
[7]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IMP AND GTP.
PubMed=12004071; DOI=10.1074/jbc.M203730200;
Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.;
"IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle
adenylosuccinate synthetase.";
J. Biol. Chem. 277:26779-26787(2002).
[8]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
PubMed=12186864; DOI=10.1074/jbc.M204952200;
Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.;
"Feedback inhibition and product complexes of recombinant mouse muscle
adenylosuccinate synthetase.";
J. Biol. Chem. 277:40536-40543(2002).
[9]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
PubMed=16981730; DOI=10.1021/bi0607498;
Iancu C.V., Zhou Y., Borza T., Fromm H.J., Honzatko R.B.;
"Cavitation as a mechanism of substrate discrimination by
adenylosuccinate synthetases.";
Biochemistry 45:11703-11711(2006).
-!- 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 committed step in the
biosynthesis of AMP from IMP. {ECO:0000269|PubMed:12482871}.
-!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_03126}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) 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.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12 uM for GTP {ECO:0000269|PubMed:12482871};
KM=45 uM for IMP {ECO:0000269|PubMed:12482871};
KM=140 uM for L-aspartate {ECO:0000269|PubMed:12482871};
pH dependence:
Optimum pH is 6.6-6.9. {ECO:0000269|PubMed:12482871};
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03126}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
protein. Note=Partially associated with particulate fractions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28650-1; Sequence=Displayed;
Name=2;
IsoId=P28650-2; Sequence=VSP_008422;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High levels in muscle.
-!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
{ECO:0000255|HAMAP-Rule:MF_03126}.
-----------------------------------------------------------------------
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EMBL; M74495; AAA82870.1; -; mRNA.
EMBL; BC039943; AAH39943.1; -; mRNA.
CCDS; CCDS26192.1; -. [P28650-1]
PIR; A39317; AJMSDS.
RefSeq; NP_031447.1; NM_007421.2. [P28650-1]
UniGene; Mm.3440; -.
PDB; 1IWE; X-ray; 2.10 A; A/B=1-457.
PDB; 1J4B; X-ray; 2.50 A; A=1-457.
PDB; 1LNY; X-ray; 2.20 A; A/B=1-457.
PDB; 1LON; X-ray; 2.10 A; A=1-457.
PDB; 1LOO; X-ray; 2.20 A; A=1-457.
PDB; 1MEZ; X-ray; 2.40 A; A=1-457.
PDB; 1MF0; X-ray; 2.50 A; A=1-457.
PDB; 1MF1; X-ray; 2.70 A; A=1-457.
PDB; 2DGN; X-ray; 2.40 A; A=1-457.
PDBsum; 1IWE; -.
PDBsum; 1J4B; -.
PDBsum; 1LNY; -.
PDBsum; 1LON; -.
PDBsum; 1LOO; -.
PDBsum; 1MEZ; -.
PDBsum; 1MF0; -.
PDBsum; 1MF1; -.
PDBsum; 2DGN; -.
ProteinModelPortal; P28650; -.
SMR; P28650; -.
BioGrid; 198010; 1.
IntAct; P28650; 2.
MINT; P28650; -.
STRING; 10090.ENSMUSP00000021726; -.
iPTMnet; P28650; -.
PhosphoSitePlus; P28650; -.
SwissPalm; P28650; -.
PaxDb; P28650; -.
PeptideAtlas; P28650; -.
PRIDE; P28650; -.
Ensembl; ENSMUST00000021726; ENSMUSP00000021726; ENSMUSG00000011148. [P28650-1]
GeneID; 11565; -.
KEGG; mmu:11565; -.
UCSC; uc007peu.2; mouse. [P28650-1]
CTD; 122622; -.
MGI; MGI:87947; Adssl1.
eggNOG; KOG1355; Eukaryota.
eggNOG; COG0104; LUCA.
GeneTree; ENSGT00390000015553; -.
HOGENOM; HOG000260959; -.
HOVERGEN; HBG053768; -.
InParanoid; P28650; -.
KO; K01939; -.
PhylomeDB; P28650; -.
BRENDA; 6.3.4.4; 3474.
Reactome; R-MMU-73817; Purine ribonucleoside monophosphate biosynthesis.
UniPathway; UPA00075; UER00335.
ChiTaRS; Adssl1; mouse.
EvolutionaryTrace; P28650; -.
PRO; PR:P28650; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000011148; -.
CleanEx; MM_ADSSL1; -.
ExpressionAtlas; P28650; baseline and differential.
Genevisible; P28650; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0051015; F:actin filament binding; ISO:MGI.
GO; GO:0004019; F:adenylosuccinate synthase activity; IDA:MGI.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
GO; GO:0006167; P:AMP biosynthetic process; ISO:MGI.
GO; GO:0006531; P:aspartate metabolic process; ISO:MGI.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
GO; GO:0046040; P:IMP metabolic process; ISO:MGI.
GO; GO:0006163; P:purine nucleotide metabolic process; IDA:MGI.
GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; ISO:MGI.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
CDD; cd03108; AdSS; 1.
HAMAP; MF_00011; Adenylosucc_synth; 1.
HAMAP; MF_03126; Adenylosucc_synth_vert_basic; 1.
InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
InterPro; IPR001114; Adenylosuccinate_synthetase.
InterPro; IPR027509; AdSS_1_vert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11846; PTHR11846; 1.
Pfam; PF00709; Adenylsucc_synt; 1.
SMART; SM00788; Adenylsucc_synt; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00184; purA; 1.
PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
GTP-binding; Ligase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Purine biosynthesis; Reference proteome.
CHAIN 1 457 Adenylosuccinate synthetase isozyme 1.
/FTId=PRO_0000095133.
NP_BIND 42 48 GTP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
NP_BIND 70 72 GTP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
NP_BIND 363 365 GTP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
NP_BIND 445 448 GTP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
REGION 43 46 IMP binding.
REGION 68 71 IMP binding.
REGION 331 337 Substrate binding.
ACT_SITE 43 43 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03126}.
ACT_SITE 71 71 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_03126}.
METAL 43 43 Magnesium.
METAL 70 70 Magnesium; via carbonyl oxygen.
BINDING 43 43 Substrate.
BINDING 163 163 IMP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
BINDING 177 177 IMP; shared with dimeric partner.
{ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
BINDING 256 256 IMP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
BINDING 271 271 IMP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
BINDING 335 335 IMP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
BINDING 337 337 GTP. {ECO:0000255|HAMAP-Rule:MF_03126,
ECO:0000269|PubMed:12004071}.
VAR_SEQ 136 136 L -> LENEVPHEPLPSASLLPMCWLLAP (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_008422.
TURN 27 29 {ECO:0000244|PDB:1J4B}.
STRAND 33 42 {ECO:0000244|PDB:1IWE}.
HELIX 46 54 {ECO:0000244|PDB:1IWE}.
STRAND 58 62 {ECO:0000244|PDB:1IWE}.
STRAND 71 74 {ECO:0000244|PDB:1IWE}.
STRAND 79 85 {ECO:0000244|PDB:1IWE}.
HELIX 87 90 {ECO:0000244|PDB:1IWE}.
STRAND 94 98 {ECO:0000244|PDB:1IWE}.
STRAND 102 104 {ECO:0000244|PDB:1IWE}.
HELIX 106 117 {ECO:0000244|PDB:1IWE}.
TURN 118 120 {ECO:0000244|PDB:1IWE}.
HELIX 124 126 {ECO:0000244|PDB:1IWE}.
STRAND 127 131 {ECO:0000244|PDB:1IWE}.
HELIX 139 155 {ECO:0000244|PDB:1IWE}.
STRAND 164 166 {ECO:0000244|PDB:1IWE}.
HELIX 167 175 {ECO:0000244|PDB:1IWE}.
HELIX 182 185 {ECO:0000244|PDB:1IWE}.
HELIX 189 205 {ECO:0000244|PDB:1IWE}.
HELIX 214 228 {ECO:0000244|PDB:1IWE}.
HELIX 229 231 {ECO:0000244|PDB:1IWE}.
HELIX 235 244 {ECO:0000244|PDB:1IWE}.
STRAND 250 253 {ECO:0000244|PDB:1IWE}.
HELIX 258 260 {ECO:0000244|PDB:1IWE}.
TURN 262 264 {ECO:0000244|PDB:1IWE}.
HELIX 278 284 {ECO:0000244|PDB:1IWE}.
HELIX 288 290 {ECO:0000244|PDB:1IWE}.
STRAND 291 304 {ECO:0000244|PDB:1IWE}.
STRAND 306 308 {ECO:0000244|PDB:1IWE}.
HELIX 317 325 {ECO:0000244|PDB:1IWE}.
TURN 331 333 {ECO:0000244|PDB:1IWE}.
STRAND 338 340 {ECO:0000244|PDB:1IWE}.
HELIX 344 354 {ECO:0000244|PDB:1IWE}.
STRAND 357 362 {ECO:0000244|PDB:1IWE}.
HELIX 364 367 {ECO:0000244|PDB:1IWE}.
STRAND 371 381 {ECO:0000244|PDB:1IWE}.
STRAND 384 388 {ECO:0000244|PDB:1LOO}.
HELIX 395 398 {ECO:0000244|PDB:1IWE}.
STRAND 400 407 {ECO:0000244|PDB:1IWE}.
HELIX 419 421 {ECO:0000244|PDB:1IWE}.
HELIX 424 437 {ECO:0000244|PDB:1IWE}.
STRAND 441 445 {ECO:0000244|PDB:1IWE}.
STRAND 447 449 {ECO:0000244|PDB:1IWE}.
TURN 450 452 {ECO:0000244|PDB:1IWE}.
STRAND 453 455 {ECO:0000244|PDB:1IWE}.
SEQUENCE 457 AA; 50254 MW; EBEC85BF907B7FED CRC64;
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL
RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY
EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA
YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA
LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE
DLPPQAQSYV RFVENHMGVA VKWVGVGKSR ESMIQLF


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