ID J3QN31_MOUSE Unreviewed; 480 AA.
AC J3QN31;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Adenylosuccinate synthetase isozyme 1 {ECO:0000256|HAMAP-Rule:MF_03126};
DE Short=AMPSase 1 {ECO:0000256|HAMAP-Rule:MF_03126};
DE Short=AdSS 1 {ECO:0000256|HAMAP-Rule:MF_03126};
DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, basic isozyme {ECO:0000256|HAMAP-Rule:MF_03126};
DE AltName: Full=Adenylosuccinate synthetase, muscle isozyme {ECO:0000256|HAMAP-Rule:MF_03126};
DE Short=M-type adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03126};
DE AltName: Full=IMP--aspartate ligase 1 {ECO:0000256|HAMAP-Rule:MF_03126};
GN Name=Adss1 {ECO:0000313|Ensembl:ENSMUSP00000136572.2,
GN ECO:0000313|MGI:MGI:87947};
GN Synonyms=ADSS1 {ECO:0000256|HAMAP-Rule:MF_03126}, ADSSL1
GN {ECO:0000256|HAMAP-Rule:MF_03126}, Adssl1 {ECO:0000313|MGI:MGI:87947};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000136572.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000136572.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000136572.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000136572.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000136572.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the purine nucleotide cycle (PNC), which
CC interconverts IMP and AMP to regulate the nucleotide levels in various
CC tissues, and which contributes to glycolysis and ammoniagenesis.
CC Catalyzes the first commited step in the biosynthesis of AMP from IMP.
CC {ECO:0000256|HAMAP-Rule:MF_03126}.
CC -!- FUNCTION: Component of the purine nucleotide cycle (PNC), which
CC interconverts IMP and AMP to regulate the nucleotide levels in various
CC tissues, and which contributes to glycolysis and ammoniagenesis.
CC Catalyzes the first committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000256|ARBA:ARBA00025042}.
CC -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC nucleotide biosynthesis. {ECO:0000256|RuleBase:RU000520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03126, ECO:0000256|RuleBase:RU000520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03126};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03126};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03126,
CC ECO:0000256|RuleBase:RU000520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_03126}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03126}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_03126, ECO:0000256|RuleBase:RU000520}.
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DR AlphaFoldDB; J3QN31; -.
DR SMR; J3QN31; -.
DR SwissPalm; J3QN31; -.
DR jPOST; J3QN31; -.
DR MaxQB; J3QN31; -.
DR PeptideAtlas; J3QN31; -.
DR ProteomicsDB; 363784; -.
DR Antibodypedia; 28209; 103 antibodies from 18 providers.
DR Ensembl; ENSMUST00000180015.9; ENSMUSP00000136572.2; ENSMUSG00000011148.15.
DR UCSC; uc011yvf.1; mouse.
DR AGR; MGI:87947; -.
DR MGI; MGI:87947; Adss1.
DR VEuPathDB; HostDB:ENSMUSG00000011148; -.
DR GeneTree; ENSGT00390000015553; -.
DR PhylomeDB; J3QN31; -.
DR TreeFam; TF300486; -.
DR UniPathway; UPA00075; UER00335.
DR ChiTaRS; Adssl1; mouse.
DR Proteomes; UP000000589; Chromosome 12.
DR Bgee; ENSMUSG00000011148; Expressed in triceps brachii and 215 other cell types or tissues.
DR ExpressionAtlas; J3QN31; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:Ensembl.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR GO; GO:0046040; P:IMP metabolic process; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1.
DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1.
DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR HAMAP; MF_03126; Adenylosucc_synth_vert_basic; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027509; AdSS_1_vert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF2; ADENYLOSUCCINATE SYNTHETASE ISOZYME 1; 1.
DR Pfam; PF00709; Adenylsucc_synt; 2.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03126};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03126};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03126};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03126};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03126};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03126};
KW Proteomics identification {ECO:0007829|EPD:J3QN31,
KW ECO:0007829|MaxQB:J3QN31};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_03126}; Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT ACT_SITE 71
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT ACT_SITE 197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134"
FT BINDING 42..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 43..46
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 68..71
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 70..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 186
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 200
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 279
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 294
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 354..360
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 358
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 386..388
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
FT BINDING 468..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03126"
SQ SEQUENCE 480 AA; 52779 MW; D3330E8A2E0C4C29 CRC64;
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG
LKDWEKRLII SDRAHLENEV PHKPLPSASL LPMCWLLAPV FDFHQAVDGL QEVQRQAQEG
KNIGTTKKGI GPTYSSKAAR TGLRICDLLS DFDEFSARFK NLAHQHQSMF PTLEIDVEGQ
LKRLKGFAER IRPMVRDGVY FMYEALHGPP KKVLVEGANA ALLDIDFGTY PFVTSSNCTV
GGVCTGLGIP PQNIGDVYGV VKAYTTRVGI GAFPTEQINE IGDLLQNRGH EWGVTTGRKR
RCGWLDLMIL RYAHMVNGFT ALALTKLDIL DVLSEIKVGI SYKLNGKRIP YFPANQEILQ
KVEVEYETLP GWKADTTGAR KWEDLPPQAQ SYVRFVENHM GVAVKWVGVG KSRESMIQLF
//
