ID   PURA_BRAJA              Reviewed;         430 AA.
AC   Q89EM1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 42.
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=bll7052;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 110;
RX   MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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; BA000040; BAC52317.1; -; Genomic_DNA.
DR   RefSeq; NP_773692.1; -.
DR   HSSP; P12283; 1ADE.
DR   GeneID; 1048009; -.
DR   GenomeReviews; BA000040_GR; bll7052.
DR   KEGG; bja:bll7052; -.
DR   NMPDR; fig|224911.1.peg.7052; -.
DR   HOGENOM; Q89EM1; -.
DR   OMA; Q89EM1; IPVCVAY.
DR   BioCyc; BJAP224911:BLL7052-MON; -.
DR   BRENDA; 6.3.4.4; 280.
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    430       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000095152.
FT   NP_BIND      12     18       GTP (Potential).
FT   ACT_SITE    141    141       By similarity.
FT   ACT_SITE    148    148       By similarity.
FT   METAL        13     13       Magnesium (By similarity).
FT   METAL        40     40       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   430 AA;  46787 MW;  6B69D4B09B13D14C CRC64;
     MANVVVVGAQ WGDEGKGKIV DWLSEQADIV VRFQGGHNAG HTLVINGKTY KLALLPSGVL
     REHKLSVIGN GVVFDPAAFL DEVTKLRAQG VAVSPENLRV AENVTLILPL HRELDAHRES
     ANAATAIGTT RRGIGPAYED KVGRRAIRLM DLADLDTLPH KIDRLLAHHN ALRRGLNLPE
     FDGKDILKEL TALAPQLLPY AETVWRLLDI KRREGKRMLF EGAQGALLDV DHGTYPYVTS
     SNTVAAQAAT GSGLGPGAVG YVLGLCKAYT TRVGQGPFPT EQDNEIGRKI GERGREFGTN
     TGRPRRCGWF DAVLVRQAVR TCGINGLALT KLDILDGFDS IEVCTGYKLD GKEIDHFPAG
     EGAQARVEPI YETIEGWKEP TASARSWADL PAQAIKYVRR IEELVGCPVA LLSTSPERED
     TILVQNPFEA
//