ID   PURA2_RALEJ             Reviewed;         452 AA.
AC   Q46QQ8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=Reut_B5180;
OS   Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
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., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-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; CP000091; AAZ64526.1; -; Genomic_DNA.
DR   RefSeq; YP_299370.1; -.
DR   GeneID; 3614614; -.
DR   GenomeReviews; CP000091_GR; Reut_B5180.
DR   KEGG; reu:Reut_B5180; -.
DR   NMPDR; fig|264198.3.peg.6155; -.
DR   HOGENOM; Q46QQ8; -.
DR   OMA; Q46QQ8; LFEGAQS.
DR   BioCyc; REUT264198:REUT_B5180-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; atypical; 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   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; FALSE_NEG.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    452       Adenylosuccinate synthetase 2.
FT                                /FTId=PRO_0000224313.
FT   METAL        20     20       Magnesium (By similarity).
FT   METAL        47     47       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   452 AA;  48972 MW;  2FBB70A36A01F41D CRC64;
     MDTATKTGYA DVLVGLQYGD EGKARVVDHL AAGYDVIARF NGGANAGHTI ATSEGILRLR
     QVPSGVLHPR VSLYIGSGCV IGLRQLASEI EMLAGQGIDL AGRLTISDRC PVVQPAHFLS
     DRRDGGRIGT TGNGIGPCYA DLAARMRGGE RSAFQLCDLM RDESRVFEQM MRLAAQRDDE
     DIAVLIQEMR QAWQVVRPFV TDNPVALLER VEGGARVLFE GAQSVMLDVV QGAQPWVTSS
     HTLPSYAYVG GDLPCRYHRK TIGVAKAMVS RVGSGPLPTE LGAERSEAYC ADAGREGRGR
     ADEAARFDPR ALLAQGDAFS TGIAIRMLSN EYGTGTGRPR RVGLLDVAQL QLAIRQFGVD
     EVYLNKCDSL AVFAQTRDRC IPVVVGSRDG NAMHVMRFPA FDESVIPRDD ATPLPPQLET
     LLEWLADVLG RPLRGIGLGP QRAQMRLFKT QP
//