ID   PURA1_RALEJ             Reviewed;         446 AA.
AC   Q46ZJ3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Adenylosuccinate synthetase 1;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase 1;
DE   AltName: Full=AdSS 1;
DE   AltName: Full=AMPSase 1;
GN   Name=purA1; OrderedLocusNames=Reut_A2076;
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 1 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.
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DR   EMBL; CP000090; AAZ61440.1; -; Genomic_DNA.
DR   RefSeq; YP_296284.1; -.
DR   GeneID; 3611744; -.
DR   GenomeReviews; CP000090_GR; Reut_A2076.
DR   KEGG; reu:Reut_A2076; -.
DR   NMPDR; fig|264198.3.peg.2762; -.
DR   HOGENOM; Q46ZJ3; -.
DR   OMA; Q46ZJ3; KAQNYIR.
DR   BioCyc; REUT264198:REUT_A2076-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    446       Adenylosuccinate synthetase 1.
FT                                /FTId=PRO_0000224312.
FT   NP_BIND      20     26       GTP (Potential).
FT   ACT_SITE    148    148       By similarity.
FT   ACT_SITE    155    155       By similarity.
FT   METAL        21     21       Magnesium (By similarity).
FT   METAL        48     48       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   446 AA;  47981 MW;  D7469D952A757324 CRC64;
     MSASAVGQGR NVVVIGTQWG DEGKGKIVDW LTDHAKGVVR FQGGHNAGHT LIIGGKKTIL
     RLIPSGIMRE GTVCYIGNGV VLSPEALFRE IEELETAGLE VQKRLRISEA ATLILPYHVA
     IDKAREARRG AAKIGTTGRG IGPAYEDKVA RRALRVQDLF DPQQFAERLR ENLDFHNFML
     TQYLGAEAVD YQQTLDDALA FAPRLAPMVA DVSAELYAVN AAGGNLMFEG AQGTLLDVDH
     GTYPFVTSSN CVAGAAAAGA GVGPGRLSYI LGITKAYCTR VGAGPFPSEL YDNDNPARQD
     QVGVRLANVG KEFGSVTGRP RRTGWLDAAA LKRSVQINGV SGLCLTKLDV LDGLESIKLC
     VGYTLDGKTV DILPRGSDAV ARCEPVYEEF PGWNESTFGV KAWDALPEAA RVYLKRVEEV
     VGIPIDMIST GPDRDETILL RHPYLA
//