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PUR8_ECOL6
ID   PUR8_ECOL6              Reviewed;         456 AA.
AC   P0AB90; P25739;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Adenylosuccinate lyase;
DE            Short=ASL;
DE            EC=4.3.2.2 {ECO:0000250|UniProtKB:P0AB89};
DE   AltName: Full=Adenylosuccinase;
DE            Short=ASase;
GN   Name=purB; OrderedLocusNames=c1510;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000250|UniProtKB:P0AB89}.
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:0000250|UniProtKB:P0AB89};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC         Evidence={ECO:0000250|UniProtKB:P0AB89};
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:0000250|UniProtKB:P0AB89};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC         Evidence={ECO:0000250|UniProtKB:P0AB89};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2.
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   -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC       catalytic and substrate-binding residues to each active site (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79979.1; -; Genomic_DNA.
DR   RefSeq; WP_000423742.1; NC_004431.1.
DR   AlphaFoldDB; P0AB90; -.
DR   SMR; P0AB90; -.
DR   STRING; 199310.c1510; -.
DR   EnsemblBacteria; AAN79979; AAN79979; c1510.
DR   KEGG; ecc:c1510; -.
DR   eggNOG; COG0015; Bacteria.
DR   HOGENOM; CLU_025566_2_0_6; -.
DR   OMA; TQVNPCD; -.
DR   BioCyc; ECOL199310:C1510-MON; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000001410; 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   Gene3D; 1.10.275.10; -; 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; IPR013539; PurB_C.
DR   Pfam; PF08328; ASL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Acetylation; Lyase; Purine biosynthesis.
FT   CHAIN           1..456
FT                   /note="Adenylosuccinate lyase"
FT                   /id="PRO_0000137879"
FT   ACT_SITE        171
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   ACT_SITE        295
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         15..16
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         90..92
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         122..123
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         247
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         296
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         301..303
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         309
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         335
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         340..344
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   MOD_RES         94
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         366
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  51543 MW;  8D1F4546B66795BC CRC64;
     MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH AAIKEVPAFA
     ADAIGYLDAI VASFSEEDAA RIKTIERTTN HDVKAVEYFL KEKVAEIPEL HAVSEFIHFA
     CTSEDINNLS HALMLKTARD EVILPYWRQL IDGIKDLAVQ YRDIPLLSRT HGQPATPSTI
     GKEMANVAYR MERQYRQLNQ VEILGKINGA VGNYNAHIAA YPEVDWHQFS EEFVTSLGIQ
     WNPYTTQIEP HDYIAELFDC VARFNTILID FDRDVWGYIA LNHFKQKTIA GEIGSSTMPH
     KVNPIDFENS EGNLGLSNAV LQHLASKLPV SRWQRDLTDS TVLRNLGVGI GYALIAYQST
     LKGVSKLEVN RDHLLDELDH NWEVLAEPIQ TVMRRYGIEK PYEKLKELTR GKRVDAEGMK
     QFIDGLALPE EEKARLKAMT PANYIGRAIT MVDELK
 
 
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