ID   PUR8_STAS1              Reviewed;         431 AA.
AC   Q49YV3;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=SSP0882;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18027.1; -; Genomic_DNA.
DR   RefSeq; YP_300972.1; -.
DR   SMR; Q49YV3; 2-430.
DR   GeneID; 3617078; -.
DR   GenomeReviews; AP008934_GR; SSP0882.
DR   KEGG; ssp:SSP0882; -.
DR   NMPDR; fig|342451.4.peg.652; -.
DR   HOGENOM; Q49YV3; -.
DR   OMA; Q49YV3; TIGRSHG.
DR   BioCyc; SSAP342451:SSP0882-MON; -.
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_0000259985.
FT   ACT_SITE     68     68       Proton donor (By similarity).
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
SQ   SEQUENCE   431 AA;  49412 MW;  0D78B0FDCDE23205 CRC64;
     MIERYSREEM SNIWTDQNRY EAWLEVEILA CEAWSKLGDI PAEDVKKIRE NAKVDVARAQ
     EIEQETRHDV VAFTRQVSET LGEERKWVHY GLTSTDVVDT ALSYVIKQAN EIIKKDLERF
     IDVLAQKAKD YKYTLMMGRT HGVHAEPTTF GVKMALWYTE MKRNLERFKQ VRKEIEVGKM
     SGAVGTFANI PPEIEAYVCE HLGLDAAPVS TQTLQRDRHA YYVATLALIS TSMEKFAVEI
     RNLQKTETRE VEEAFAKGQK GSSAMPHKRN PIGSENITGI ARVIRGYVTT AYENVPLWHE
     RDISHSSAER IMLPDVTIAL DYGLNRFTNI VERLTVFEDN MLANIDKTFG LIYSQRVLLA
     LINKGLAREA AYDKVQPKAM ESWETKTPFR TLIEEDATIT DLLTKEDLDE CFNPKHHLNQ
     VDTIFQRAGL E
//