ID   E9Q3T7_MOUSE            Unreviewed;       425 AA.
AC   E9Q3T7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Adenylosuccinate lyase {ECO:0000313|Ensembl:ENSMUSP00000131998.2};
GN   Name=Adsl {ECO:0000313|Ensembl:ENSMUSP00000131998.2,
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:ENSMUSP00000131998.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000131998.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131998.2,
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:ENSMUSP00000131998.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131998.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- 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   -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC       catalytic and substrate-binding residues to each active site.
CC       {ECO:0000256|ARBA:ARBA00011668}.
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DR   AlphaFoldDB; E9Q3T7; -.
DR   SMR; E9Q3T7; -.
DR   jPOST; E9Q3T7; -.
DR   MaxQB; E9Q3T7; -.
DR   PeptideAtlas; E9Q3T7; -.
DR   ProteomicsDB; 361188; -.
DR   Antibodypedia; 34889; 288 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000164806.6; ENSMUSP00000131998.2; ENSMUSG00000022407.11.
DR   AGR; MGI:103202; -.
DR   MGI; MGI:103202; Adsl.
DR   VEuPathDB; HostDB:ENSMUSG00000022407; -.
DR   GeneTree; ENSGT00950000183122; -.
DR   HOGENOM; CLU_030949_1_1_1; -.
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; E9Q3T7; 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; 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; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:E9Q3T7,
KW   ECO:0007829|MaxQB:E9Q3T7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          98..308
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
SQ   SEQUENCE   425 AA;  48297 MW;  A8959972D3E794D0 CRC64;
     MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE QTLGLPITDE
     QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD
     LIILRNAFDL LLPKLARVIS RLADFAKDRA DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC
     MDLQNLKRVR DELRFRGVKG TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG
     QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
     SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE
     GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQVHR FLEEEVRPLL KPYGNEMAVK
     AELCL
//