ID   PURA_BAUCH              Reviewed;         432 AA.
AC   Q1LSQ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=BCI_0577;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14350.1; -; Genomic_DNA.
DR   RefSeq; YP_589005.1; -.
DR   SMR; Q1LSQ9; 3-430.
DR   GeneID; 4056248; -.
DR   GenomeReviews; CP000238_GR; BCI_0577.
DR   KEGG; bci:BCI_0577; -.
DR   HOGENOM; Q1LSQ9; -.
DR   OMA; Q1LSQ9; YVLGIIK.
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_1000000782.
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;  47694 MW;  49C1EE07FBA92D21 CRC64;
     MSNNVVVLGT QWGDEGKGKV VDILTERAKY VIRYQGGHNA GHTLVINGEK TILHLIPSGI
     LRENVKSIIA HGVVLSPEAL IKEIHELEAR GIPVRQRMLI SEACPLLLSY HVAMDIAREK
     ARGTNALGTT GRGIGPAYED KVARRALRVS DLFNKESFAI KLKDIVDYYN FQLVHYYKVE
     AVSYQKILND IMVVTDMLTS MVADISVLLY NAYQQGDIMM FEGAQGTLLD IDHGTYPYVT
     SSNTTAGCVT TGSGLGPHYI GYVLGIVKAY STRVGAGPFP TELFDDTGNF LCLKGHEFGA
     TTGRRRRTGW LDAVALRRAV HINSISGLCL TKLDVLDGLK EIKICSAYRM QDGCIIYTTP
     IALEKWEGIE PIYETLPGWN ETTVGIQALA DLPRAAHQYI KLIEELTRVP VDIISTGPDR
     RDTIILHDPF SD
//