ID   PURA_BRUSU              Reviewed;         429 AA.
AC   P65879; Q8FZ20; Q8YIU1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=BR1683;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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; AE014291; AAN30583.1; -; Genomic_DNA.
DR   RefSeq; NP_698668.1; -.
DR   HSSP; P12283; 1ADE.
DR   GeneID; 1167376; -.
DR   GenomeReviews; AE014291_GR; BR1683.
DR   KEGG; bms:BR1683; -.
DR   TIGR; BR1683; -.
DR   HOGENOM; P65879; -.
DR   OMA; P65879; IPVCVAY.
DR   BioCyc; BSUI204722:BR_1683-MON; -.
DR   BRENDA; 6.3.4.4; 281610.
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    429       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000095156.
FT   NP_BIND      12     18       GTP (Potential).
FT   ACT_SITE    140    140       By similarity.
FT   ACT_SITE    147    147       By similarity.
FT   METAL        13     13       Magnesium (By similarity).
FT   METAL        40     40       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   429 AA;  46561 MW;  DF90E83E30690FF2 CRC64;
     MANVVVVGSQ WGDEGKGKIV DWLSERADVI VRYQGGHNAG HTLVIDGVSY KLSLLPSGLV
     RGKLSVIGNG VVVDPHHFVA EVEKLRGQGI DVTPDVLRVA ENAPLILSIH RELDAMREGS
     NSGLKIGTTK RGIGPAYEDK VGRRAIRVID LTEPETLRPK VERLLAHHNS LRRGMGLEEI
     AVETILTELT SVADQILPYI DQVWRVLDER RKAGARILFE GAQGALLDND HGTYPFVTSS
     NTVAGQAAAG SGLGPTAIGY VLGITKAYTT RVGEGPFPTE LNDEIGEFLG TKGHEFGVVT
     GRKRRCGWFD AVIVRQTVRT SGINGIALTK LDVLDGLEEI KICVAYELDG KRIDYLPSSM
     GAQARVKPIY ETLPGWSETT AGARSWNDLP AQAVKYVRHI EELIGAPVAM LSTSPEREDT
     ILVTDPFHD
//