ID   E9Q242_MOUSE            Unreviewed;       469 AA.
AC   E9Q242;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172};
DE            Short=ASL {ECO:0000256|RuleBase:RU361172};
DE            EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172};
GN   Name=Adsl {ECO:0000313|Ensembl:ENSMUSP00000127593.2,
GN   ECO:0000313|MGI:MGI:103202};
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:ENSMUSP00000127593.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000127593.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000127593.2,
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:ENSMUSP00000127593.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000127593.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes two non-sequential steps in de novo AMP synthesis:
CC       converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
CC       carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamide, and thereby also contributes to de
CC       novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP)
CC       to AMP and fumarate. {ECO:0000256|ARBA:ARBA00002971}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC         carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920,
CC         ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000598,
CC         ECO:0000256|RuleBase:RU361172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
CC         Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
CC         ChEBI:CHEBI:456215; EC=4.3.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000811,
CC         ECO:0000256|RuleBase:RU361172};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC       catalytic and substrate-binding residues to each active site.
CC       {ECO:0000256|ARBA:ARBA00011668}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|RuleBase:RU361172}.
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DR   AlphaFoldDB; E9Q242; -.
DR   SMR; E9Q242; -.
DR   jPOST; E9Q242; -.
DR   MaxQB; E9Q242; -.
DR   PeptideAtlas; E9Q242; -.
DR   ProteomicsDB; 351742; -.
DR   Antibodypedia; 34889; 288 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000168756.8; ENSMUSP00000127593.2; ENSMUSG00000022407.11.
DR   AGR; MGI:103202; -.
DR   MGI; MGI:103202; Adsl.
DR   VEuPathDB; HostDB:ENSMUSG00000022407; -.
DR   GeneTree; ENSGT00950000183122; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   ChiTaRS; Adsl; mouse.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000022407; Expressed in hindlimb stylopod muscle and 284 other cell types or tissues.
DR   ExpressionAtlas; E9Q242; baseline and differential.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03302; Adenylsuccinate_lyase_2; 1.
DR   Gene3D; 1.10.275.60; -; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR004769; Pur_lyase.
DR   NCBIfam; TIGR00928; purB; 1.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   Lyase {ECO:0000256|RuleBase:RU361172};
KW   Proteomics identification {ECO:0007829|EPD:E9Q242,
KW   ECO:0007829|MaxQB:E9Q242};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          362..446
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   469 AA;  53130 MW;  56CAD8A1FCF88727 CRC64;
     MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE QTLGLPITDE
     QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTL
     ARVISRLADF AKDRADLPTL GFTHFQPAQL TTVGKRCCLW IQDLCMDLQN LKRVRDELRF
     RGVKGTTGTQ ASFLQLFEGD HQKVEQLDKM VTEKAGFKRA FIITGQTYTR KVDIEVLSVL
     ASLGASVHKI CTDIRLLANL KEMEEPFEKQ QIGSSAMPYK RNPMRSERCC SLARHLMALT
     MDPLQTASVQ WFERTLDDSA NRRICLAEAF LTADTILNTL QNISEGLVVY PKVIERRIRQ
     ELPFMATENI IMAMVKAGGS RQDCHEKIRV LSQQAAAVVK QEGGDNDLIE RIRADAYFSP
     IHSQLEHLLD PSSFTGRAPQ QVHRFLEEEV RPLLKPYGNE MAVKAELCL
//