ID   PURA_ANAVT              Reviewed;         447 AA.
AC   Q3MBG1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=Ava_2053;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
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., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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.
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; CP000117; ABA21675.1; -; Genomic_DNA.
DR   RefSeq; YP_322570.1; -.
DR   GeneID; 3680702; -.
DR   GenomeReviews; CP000117_GR; Ava_2053.
DR   KEGG; ava:Ava_2053; -.
DR   NMPDR; fig|240292.3.peg.3133; -.
DR   HOGENOM; Q3MBG1; -.
DR   OMA; Q3MBG1; IPVCVAY.
DR   BioCyc; AVAR240292:AVA_2053-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    447       Adenylosuccinate synthetase.
FT                                /FTId=PRO_1000000775.
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   447 AA;  49140 MW;  C45B513FAEB7AC80 CRC64;
     MANVIVIGAQ WGDEGKGKIT DLLSRSADVV VRYQGGVNAG HTIVVKGQTF KLHLIPSGIL
     YPDTECMIGC GTVIDPQVLI KELDQLESLN ISTKNLLISE TAHVTMPYHR LIDKASEERR
     GSHKIGTTGR GIGPTYADKS ERTGIRVLDL MDPAALRDQL AWTINNKNLI LEKLYNLPPL
     DTEEVVKEYL GYAERLRPHV VDTSLKIYDA IQRRRNILFE GAQGTLLDLD HGTYPYVTSS
     NPVAGGACVG TGLGPTMIDR VIGVSKAYTT RVGEGPFPTE LDGELGELLC DRGAEFGTTT
     GRKRRCGWFD AVIGRYAVRI NGMDCMAITK LDVLDELEEI QVCIAYEIDG DRCDHFPTSA
     RQFARCRPIY KTLPGWQVPT SECRTLEDLP QQALDYLKFL AELMEVPIAI VSLGASRDQT
     IIVEDPIHGP KRALLHPDGT PASLLSA
//