ID   PUR8_STAAC              Reviewed;         431 AA.
AC   Q5HEL4;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SACOL1969;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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: Homodimer and homotetramer. Residues from neighboring subunits
CC       contribute catalytic and substrate-binding residues to each active site
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000046; AAW36939.1; -; Genomic_DNA.
DR   RefSeq; WP_000572878.1; NC_002951.2.
DR   AlphaFoldDB; Q5HEL4; -.
DR   SMR; Q5HEL4; -.
DR   EnsemblBacteria; AAW36939; AAW36939; SACOL1969.
DR   KEGG; sac:SACOL1969; -.
DR   HOGENOM; CLU_030949_0_1_9; -.
DR   OMA; ASSCEKI; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000000530; 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; 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   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Lyase; Purine biosynthesis.
FT   CHAIN           1..431
FT                   /note="Adenylosuccinate lyase"
FT                   /id="PRO_0000259974"
FT   ACT_SITE        141
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   ACT_SITE        262
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         4..5
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         67..69
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         93..94
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         212
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         263
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         268..270
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         276
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         307..311
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
SQ   SEQUENCE   431 AA;  49603 MW;  493F79CBE814B9E5 CRC64;
     MIERYSREEM SNIWTDQNRY EAWLEVEILA CEAWSELGHI PKADVQKIRQ NAKVNVERAQ
     EIEQETRHDV VAFTRQVSET LGEERKWVHY GLTSTDVVDT ALSFVIKQAN DIIEKDLERF
     IDVLAEKAKN YKYTLMMGRT HGVHAEPTTF GVKMALWYTE MQRNLQRFKQ VREEIEVGKM
     SGAVGTFANI PPEIESYVCK HLGIGTAPVS TQTLQRDRHA YYIATLALIA TSLEKFAVEI
     RNLQKTETRE VEEAFAKGQK GSSAMPHKRN PIGSENITGI SRVIRGYITT AYENVPLWHE
     RDISHSSAER IMLPDVTIAL DYALNRFTNI VDRLTVFEDN MRNNIDKTFG LIFSQRVLLA
     LINKGMVREE AYDKVQPKAM ISWETKTPFR ELIEQDESIT SVLTKEELDE CFDPKHHLNQ
     VDTIFERAGL A