ID   B4DEP1_HUMAN            Unreviewed;       127 AA.
AC   B4DEP1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   04-NOV-2026, entry version 102.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058};
DE            EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG57152.1};
RN   [1] {ECO:0000313|EMBL:BAG57152.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAG57152.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = fumarate + AMP;
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:ARBA00047513};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2. {ECO:0000256|ARBA:ARBA00004734}.
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|ARBA:ARBA00004706}.
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|ARBA:ARBA00008273}.
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DR   EMBL; AK293722; BAG57152.1; -; mRNA.
DR   SMR; B4DEP1; -.
DR   ProteomicsDB; 3975; -.
DR   UCSC; uc062emv.1; human.
DR   VEuPathDB; HostDB:ENSG00000239900; -.
DR   OrthoDB; 406045at2759; -.
DR   ChiTaRS; ADSL; human.
DR   Bgee; ENSG00000239900; Expressed in hindlimb stylopod muscle and 100 other cell types or tissues.
DR   FunFam; 1.10.275.60:FF:000001; Adenylosuccinate lyase; 1.
DR   Gene3D; 1.10.275.60; -; 1.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   AlphaFoldDB; B4DEP1; -.
PE   1: Evidence at protein level;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:BAG57152.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
SQ   SEQUENCE   127 AA;  14285 MW;  9CBCBB5C464C4A86 CRC64;
     MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE QTLGLPITDE
     QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTV
     GACVVYT
//