ID   E1Q345_HELPP            Unreviewed;       440 AA.
AC   E1Q345;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058, ECO:0000256|RuleBase:RU361172};
DE            Short=ASL {ECO:0000256|RuleBase:RU361172};
DE            EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339, ECO:0000256|RuleBase:RU361172};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717, ECO:0000256|RuleBase:RU361172};
GN   OrderedLocusNames=HPPC_05405 {ECO:0000313|EMBL:ADO07293.1};
OS   Helicobacter pylori (strain PeCan4).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=765963 {ECO:0000313|EMBL:ADO07293.1, ECO:0000313|Proteomes:UP000006863};
RN   [1] {ECO:0000313|Proteomes:UP000006863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PeCan4 {ECO:0000313|Proteomes:UP000006863};
RA   Kersulyte D., Vasquez J., Gilman R.H., Berg D.E.;
RT   "Complete genome sequence of Helicobacter pylori strain PeCan4.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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:ARBA00024477};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC         Evidence={ECO:0000256|ARBA:ARBA00024477};
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:ARBA00024487};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC         Evidence={ECO:0000256|ARBA:ARBA00024487};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2. {ECO:0000256|ARBA:ARBA00004734,
CC       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|ARBA:ARBA00004706, ECO:0000256|RuleBase:RU361172}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|ARBA:ARBA00008273,
CC       ECO:0000256|RuleBase:RU361172}.
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DR   EMBL; CP002074; ADO07293.1; -; Genomic_DNA.
DR   RefSeq; WP_000893889.1; NC_014555.1.
DR   AlphaFoldDB; E1Q345; -.
DR   KEGG; hpc:HPPC_05405; -.
DR   HOGENOM; CLU_030949_0_1_7; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000006863; Chromosome.
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; cd01360; Adenylsuccinate_lyase_1; 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   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR024083; Fumarase/histidase_N.
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; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:ADO07293.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|RuleBase:RU361172}.
FT   DOMAIN          349..439
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   440 AA;  49901 MW;  CEA05672E00044B3 CRC64;
     MLERYANEEM KALWNEQTKF ETYLEVEKAV VRAWNKLGQI QDSDCEKICS KAAFNLERIK
     EIEKTTKHDL IAFTTCVAES LGEESRFFHY GITSSDCIDT AMALLMTKSL KLIQKGVKNL
     YETLKNRALE HKDTLMVGRS HGVFGEPITF GLVLALFADE IKRHLKALDL TMEFISVGAI
     SGAMGNFAHA PLELEELACE FLGLKTANIS NQVIQRDRYA RLACDLALLA SSCEKIAVNI
     RHLQRSEVYE VEEAFSAGQK GSSAMPHKRN PILSENITGL CRVIRSFTTP MLENVALWHE
     RDMSHSSVER FALPDLFITS DFMLSRLNSV IENLVVYPKN MLKNLALSGG LVFSQRVLLE
     LPKKGLSREE SYSIVQENAM KIWEILQQGA FKNADENLFL NALLNDERLK KYLSEDEIKA
     CFDYSYYTKN VGAIFKRVFG
//