ID   PURA_BLOPB              Reviewed;         432 AA.
AC   Q494F3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Adenylosuccinate synthetase;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase;
DE   AltName: Full=AdSS;
DE   AltName: Full=AMPSase;
GN   Name=purA; OrderedLocusNames=BPEN_086;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis.
CC   -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
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DR   EMBL; CP000016; AAZ40729.1; -; Genomic_DNA.
DR   RefSeq; YP_277601.1; -.
DR   GeneID; 3563190; -.
DR   GenomeReviews; CP000016_GR; BPEN_086.
DR   KEGG; bpn:BPEN_086; -.
DR   HOGENOM; Q494F3; -.
DR   OMA; Q494F3; YVLGIIK.
DR   BioCyc; CBLO291272:BPEN_086-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00011; -; 1.
DR   InterPro; IPR018220; Adenylosuccinate_synthase_AS.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   PANTHER; PTHR11846; Asucc_synthtase; 1.
DR   Pfam; PF00709; Adenylsucc_synt; 1.
DR   ProDom; PD001188; Asucc_synthtase; 1.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   TIGRFAMs; TIGR00184; purA; 1.
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    432       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000224260.
FT   NP_BIND      13     19       GTP (Potential).
FT   ACT_SITE    141    141       By similarity.
FT   ACT_SITE    148    148       By similarity.
FT   METAL        14     14       Magnesium (By similarity).
FT   METAL        41     41       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   432 AA;  48034 MW;  F4510D50AEB4FD3A CRC64;
     MARSIVVLGA QWGDEGKGKI VDWLTSRAQY VVRYQGGHNA GHTIVVDQQK ITLHLIPSGI
     LHNHVTAVIA NGVVLSPFSL IKEMKMLLKL GVSTCKRIFI SASCPLLLPY HVAMDLAREN
     HHISKAIGTT GCGIGPSYED KVARRALRVS DLYNLKYFKN KLKDVVDYYN FQLVYYYKTK
     PINYQIVLEE VMSISDILID MVVDVPELLD DAAKRGDSVI FEGAQGSLLD IDHGTYPYVT
     SSHTIAGSVS VGAGVGLNYI DYVLGIVKAY STRVGFGPFP TELSNDTGNW LCMNGNEFGS
     TTGRRRRTGW FDAVSVRYSV KINSFFSCCL TKIDVLDGLK ELKICIAYRK KNGKVIHNFP
     CSLEELENCV PIYEILPGWM ISTVGITEFH QLPKESQLYV KRIEELIGVP IHIVSTGSDR
     SAIIILRNPF DS
//