ID   PURA_ALCBS              Reviewed;         430 AA.
AC   Q0VMF3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=ABO_2197;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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.
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DR   EMBL; AM286690; CAL17645.1; -; Genomic_DNA.
DR   RefSeq; YP_693917.1; -.
DR   GeneID; 4211140; -.
DR   GenomeReviews; AM286690_GR; ABO_2197.
DR   KEGG; abo:ABO_2197; -.
DR   NMPDR; fig|393595.12.peg.2197; -.
DR   HOGENOM; Q0VMF3; -.
DR   OMA; Q0VMF3; YVLGIIK.
DR   BioCyc; ABOR393595:ABO_2197-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    430       Adenylosuccinate synthetase.
FT                                /FTId=PRO_1000000771.
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   430 AA;  46611 MW;  13D93C906D4FF4BA CRC64;
     MGKNVVILGT QWGDEGKGKI VDLLTDQASL VARFQGGHNA GHTLVIDGKK TVLHLIPSGI
     LREDVQCLIG NGVVLSLEAL LKEIGGLEDQ GVPVRDRLRL SASCPLILPV HVALDQAREA
     ARGNKKIGTT GRGIGPAYED KVARRGLRLG DVYQRELFAA KLGEVMDYHN FVLRSYYNAE
     PVDFQKTLDD TLQLGEDVRS MVTDVTAVLH GARERGENIM FEGAQGTLLD IDHGTYPYVT
     SSNTTAGGTA TGTGFGPLYL DYVLGITKAY TTRVGSGPFP TELFDENGRY LAEKGHEFGS
     TTGRARRCGW FDAVALKRSI QINSITGLCL TKLDVLDGLE EINICVGYQD AAGNSLECAW
     DADSYEEVKP VYESLPGWSE STLGVKSEDD LPPNAKAYLK RIEAITGAPI DIISTGPDRV
     ETIIKRHPFS
//