ID   E6XNB5_SHEP2            Unreviewed;       456 AA.
AC   E6XNB5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=Sput200_2258 {ECO:0000313|EMBL:ADV54705.1};
OS   Shewanella putrefaciens (strain 200).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV54705.1, ECO:0000313|Proteomes:UP000008209};
RN   [1] {ECO:0000313|EMBL:ADV54705.1, ECO:0000313|Proteomes:UP000008209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200 {ECO:0000313|EMBL:ADV54705.1,
RC   ECO:0000313|Proteomes:UP000008209};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA   Fredrickson J.K., Woyke T.;
RT   "Complete sequence of Shewanella putrefaciens 200.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC       biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC       succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC       D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC       carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC       ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC       (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC       and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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; CP002457; ADV54705.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6XNB5; -.
DR   KEGG; shp:Sput200_2258; -.
DR   PATRIC; fig|399804.5.peg.2342; -.
DR   HOGENOM; CLU_025566_2_0_6; -.
DR   OrthoDB; 9768878at2; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000008209; 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; cd01598; PurB; 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; 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   InterPro; IPR047136; PurB_bact.
DR   InterPro; IPR013539; PurB_C.
DR   NCBIfam; TIGR00928; purB; 1.
DR   PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR   Pfam; PF08328; ASL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361172};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW   ECO:0000256|RuleBase:RU361172}.
FT   DOMAIN          14..312
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          331..445
FT                   /note="Adenylosuccinate lyase PurB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08328"
SQ   SEQUENCE   456 AA;  50925 MW;  B0E39F95D9294808 CRC64;
     MDLSALTAIS PVDGRYGSKT ASLRGIFSEF GLTKYRVQVE INWLKLLADC PEIIEVPPLS
     ESAIAVLDGI KDNFNEQDAL RVKAIESTTN HDVKAVEYFI KEKIAGNAEL AAVGEFVHFA
     CTSEDINNLS HGLMLTEARE QVLLPYCNEL LTAIKKLAIE YRSVPLMSRT HGQPASPSTL
     GKEMANVAVR LERQIKQIAN VEIMGKLNGA VGNYNAHLSA YPEVNWHELS ERFVTSLGLN
     WNAYTTQIEP HDYIAELFDA VARFNTVLID FDRDIWGYIA LGHFKQRTIA GEIGSSTMPH
     KVNPIDFENS EGNLGIANAL MQHLASKLPV SRWQRDLTDS TVLRNLGVGI AHALIAYQAT
     LKGISKLEVN EAHLRDELDH NWEVLAEPVQ TVMRRYGIEK PYEKLKELTR GKRIDAQQLS
     VFIDGLELPD SVKAELKKMT PANYIGRAET FVDELK
//