ID   PUR8_STAA3              Reviewed;         431 AA.
AC   Q2FFI7;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Adenylosuccinate lyase;
DE            Short=ASL;
DE            EC=4.3.2.2;
DE   AltName: Full=Adenylosuccinase;
DE            Short=ASase;
GN   Name=purB; OrderedLocusNames=SAUSA300_1889;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
CC   -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-
CC       (5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 2/2.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 5/5.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily.
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DR   EMBL; CP000255; ABD20399.1; -; Genomic_DNA.
DR   RefSeq; YP_494541.1; -.
DR   SMR; Q2FFI7; 2-430.
DR   GeneID; 3914957; -.
DR   GenomeReviews; CP000255_GR; SAUSA300_1889.
DR   KEGG; saa:SAUSA300_1889; -.
DR   HOGENOM; Q2FFI7; -.
DR   OMA; Q2FFI7; HPIDFRY.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imida...; IEA:EC.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumar...; IEA:EC.
DR   GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR019468; Adenylosuccinate_lyase_C.
DR   InterPro; IPR003031; D_crystallin.
DR   InterPro; IPR000362; Fumarate_lyase.
DR   InterPro; IPR004769; Pur_lyase.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; DCRYSTALLIN.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lyase; Purine biosynthesis.
FT   CHAIN         1    431       Adenylosuccinate lyase.
FT                                /FTId=PRO_0000259981.
FT   ACT_SITE     68     68       Proton donor (By similarity).
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
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
//