ID   PURA2_PHOLL             Reviewed;         432 AA.
AC   Q7MAX9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Adenylosuccinate synthetase 2;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase 2;
DE   AltName: Full=AdSS 2;
DE   AltName: Full=AMPSase 2;
GN   Name=purA2; OrderedLocusNames=plu4577;
OS   Photorhabdus luminescens subsp. laumondii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=141679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TT01;
RX   MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S.,
RA   Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V.,
RA   Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571874; CAE16949.1; -; Genomic_DNA.
DR   RefSeq; NP_931741.1; -.
DR   SMR; Q7MAX9; 2-432.
DR   GeneID; 2804601; -.
DR   GenomeReviews; BX470251_GR; plu4577.
DR   KEGG; plu:plu4577; -.
DR   NMPDR; fig|243265.1.peg.4364; -.
DR   PhotoList; plu4577; -.
DR   HOGENOM; Q7MAX9; -.
DR   OMA; Q7MAX9; YVLGIIK.
DR   BioCyc; PLUM243265:PLU4577-MON; -.
DR   BRENDA; 6.3.4.4; 308689.
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 2.
FT                                /FTId=PRO_0000095208.
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;  47240 MW;  B798323C9425F2CA CRC64;
     MGKNVVVLGT QWGDEGKGKI VDLLTERAKY VVRYQGGHNA GHTLVINGEK TVLHLIPSGI
     LRENVISIIA NGVVLAPDAL MKEMNALESR GIPVRERLLI SEACPLILPY HVALDNAREK
     ARGAKAIGTT GRGIGPAYED KVARRGLRVG DLFDKEAFAV KLKEIIEYHN FQLVNYYKEP
     AVDYQKTLDE IMAVADILTD MVVDVSDLLY KATQKGELVM FEGAQGTLLD IDHGTYPYVT
     SSNTTAGGVA TGSGLGPCYV DYVLGIIKAY STRVGAGPFP TELFDETGGY LREKGQEFGA
     TTGRSRRTGW LDIIAIRRAV QINSLSGFCM TKLDVLDGLK EVKICTGYRM PDGSVIETTP
     LAADDWEGIE PVYETMPGWN ESTFGVKEHR KLPQAALNYI KRVEELTGVP VDIISTGPDR
     SETIILRDPF DA
//