ID   PURA_ALHEH              Reviewed;         432 AA.
AC   Q0AB55;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Mlg_0578;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000453; ABI55932.1; -; Genomic_DNA.
DR   RefSeq; YP_741422.1; -.
DR   GeneID; 4268311; -.
DR   GenomeReviews; CP000453_GR; Mlg_0578.
DR   KEGG; aeh:Mlg_0578; -.
DR   NMPDR; fig|187272.6.peg.551; -.
DR   HOGENOM; Q0AB55; -.
DR   OMA; Q0AB55; 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_1000000772.
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;  47105 MW;  A71F370D4DA93DAE CRC64;
     MAKNVVVVGS QWGDEGKGKV VDLLTEHTGA VVRFQGGHNA GHTLVIDGEQ TILHLIPSGV
     LREGVQCLIG NGVVLAPDAL LEEVQELEGK GVPARERLRI SPACPLILPC HVALDKAREA
     ARGQARIGTT GRGIGPAYED KVSRRGIRVA DLFHRERLAA KLGELLDYHN FVLQHYFHEQ
     PIDFQDVLER CLTYADELRP MVADIGQLLQ EHMDAGRDLL FEGAQGTLLD IDHGTYPFVT
     SSNTVAGAAA TGTGIGPRDL HYVLGITKAY TTRVGSGPFP TELEDEIGDL LGERGREFGA
     TTGRKRRCGW FDAVALRRAA QINSLSGLCI TKLDVLDELE TLRICIGYQC GDQLWESLPP
     GAELLADCEP QYIDLPGWQS STLGVQQWDD LPENARAYLR KLEELIGVPV AIVSTGPDRK
     ETIVLQNPFE SA
//