ID   PURA_ARTAT              Reviewed;         429 AA.
AC   A1R2A8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=AAur_0563;
OS   Arthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of
RT   Arthrobacter aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000474; ABM06751.1; -; Genomic_DNA.
DR   RefSeq; YP_946370.1; -.
DR   GeneID; 4639161; -.
DR   GenomeReviews; CP000474_GR; AAur_0563.
DR   KEGG; aau:AAur_0563; -.
DR   TIGR; AAur_0563; -.
DR   OMA; A1R2A8; IPVCVAY.
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_1000000776.
FT   NP_BIND      12     18       GTP (Potential).
FT   ACT_SITE    139    139       By similarity.
FT   ACT_SITE    146    146       By similarity.
FT   METAL        13     13       Magnesium (By similarity).
FT   METAL        40     40       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   429 AA;  46646 MW;  03BEEE52F12A8991 CRC64;
     MPAIVIVGAQ WGDEGKGKAT DLLGGRVDYV VKPNGGNNAG HTVVVGGEKY ELKLLPAGIL
     SPNAIPIIGN GCVVNLEALF QEIDGLEARG ADTSRLRVSA NAHLVAPYHQ VLDKVTERFL
     GSRAIGTTGR GIGPAYMDKV ARLGIRVQDV FDESILRQKV EGSLRQKNEL LVKVYNRRDI
     IADEIVEYFL SFAERLRPLV IDSTLELNNA LDEGKVVLME GGQATFLDVD HGTYPFVTSS
     NPTAGGASVG SGIGPTRISR SIGIIKAYTT RVGAGPFPTE LFDEMGVYLQ KTGGEFGVNT
     GRPRRCGWYD AVLARHASRV NGFTDYFVTK LDVLTGIEQI PVCVAYDVDG VRHDEMPMTQ
     TEFHHAVPIF EYFDGWTEDI TGARTLEDLP ENARNYVLAL EKLSGTRFSA IGVGPDRDQT
     IVVHDLIND
//