ID   PURA_ANADE              Reviewed;         432 AA.
AC   Q2IQF7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=Adeh_1265;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC81039.1; -; Genomic_DNA.
DR   RefSeq; YP_464476.1; -.
DR   GeneID; 3888698; -.
DR   GenomeReviews; CP000251_GR; Adeh_1265.
DR   KEGG; ade:Adeh_1265; -.
DR   HOGENOM; Q2IQF7; -.
DR   OMA; Q2IQF7; YVLGIIK.
DR   BioCyc; ADEH290397:ADEH_1265-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_1000000773.
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   432 AA;  46695 MW;  8AD767ABEC7887F2 CRC64;
     MPNVVVVGAQ WGDEGKGKIV DLLTQYADVV VRFQGGNNAG HTLVVGGEKT VLHLIPSGIL
     HPGKSCVIGN GVVIDPEVLV LEIDRLKAKG ALKDDGQLVV SLDAHVIMPW HKAIDVAREQ
     AMGEGKIGTT GRGIGPTYED KVARRGLRIR DLLDEARLAR KVKERAALAR EELARLGAKL
     ELDEPALVKR YAELGRRVAG YATDVSIWLH RALQQGKSLL FEGAQGTMLD VDHGTYPFVT
     SSNTVAGNAV VGCGLGPTAV DYVLGISKAY STRVGGGPYP TELKDETGER LRKIGGEYGA
     TTGRPRRTGW LDALALRYAV RVNGLSGIAM TKLDVLTGFD TVKIAVGYRL DGKVLDEMPS
     DPEVIERCTP VYEELPGWTE KLEHLRTWDD LPPRARAYVK RVEELAGVKV VGCSVGADRG
     ETILVENPFL AR
//