ID   PUR8_STAHJ              Reviewed;         431 AA.
AC   Q4L7M3;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=SH1043;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP006716; BAE04352.1; -; Genomic_DNA.
DR   RefSeq; YP_252958.1; -.
DR   SMR; Q4L7M3; 2-430.
DR   GeneID; 3481954; -.
DR   GenomeReviews; AP006716_GR; SH1043.
DR   KEGG; sha:SH1043; -.
DR   NMPDR; fig|279808.3.peg.1757; -.
DR   HOGENOM; Q4L7M3; -.
DR   OMA; Q4L7M3; HPIDFRY.
DR   BioCyc; SHAE279808:SH1043-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_0000259984.
FT   ACT_SITE     68     68       Proton donor (By similarity).
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
SQ   SEQUENCE   431 AA;  49894 MW;  88C7A78DF1E97747 CRC64;
     MIDRYSREEM ANIWTDQNRY EAWLEVEILA CEAWSELGHI PKEDVKKIRQ NAKVDVKRAQ
     EIEQETRHDV VAFTRQVSET LGDERKWVHY GLTSTDVVDT ALSYVIKQAN EIIEKDIERF
     IKVLEEKAKN YKYTLMMGRT HGVHAEPTTF GVKMALWYTE MKRNLKRFKE VRKEIEVGKM
     SGAVGTFANI PPEIEQYVCD HLGIDTASVS TQTLQRDRHA YYIATLALVA TSLEKFAVEI
     RNLQKTETRE VEEAFAKGQK GSSAMPHKRN PIGSENITGI SRVIRGYITT AYENVPLWHE
     RDISHSSAER IMLPDVTIAL DYALNRFTNI VDRLTVFEDN MRNNIDKTFG LIFSQRVLLA
     LINKGMVREE AYDRVQPKAM ESWETKTPFR QLIEKDESIT NVLSKEELDE CFNPEHHLNQ
     VDTIFKRAGL E
//