ID   PURA_BART1              Reviewed;         429 AA.
AC   A9IQ57;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   16-JUN-2009, entry version 12.
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=BT_0567;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems
RT   as host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis (By similarity).
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; AM260525; CAK01015.1; -; Genomic_DNA.
DR   RefSeq; YP_001609010.1; -.
DR   GeneID; 5829648; -.
DR   GenomeReviews; AM260525_GR; BT_0567.
DR   OMA; A9IQ57; ERDDTIV.
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    429       Adenylosuccinate synthetase.
FT                                /FTId=PRO_1000073937.
FT   NP_BIND      12     18       GTP (Potential).
FT   ACT_SITE    140    140       By similarity.
FT   ACT_SITE    147    147       By similarity.
FT   METAL        13     13       Magnesium (By similarity).
FT   METAL        40     40       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   429 AA;  47190 MW;  007509CECE4632D3 CRC64;
     MANVVVVGTQ WGDEGKGKIV DWLSERADIV VRYQGGHNAG HTLVIDGVSY KLSLLPSGLV
     RGKLSIIGNG VVVDPHHFVA ELKKLCDQGV KITPEILRIA ENAPLILSLH RDLDAIRESG
     LSGLKIGTTK RGIGPAYEDK VGRRAIRVMD LAEKDTLMAK IERLLRHHNA LRRGMGVAEI
     DSQALYDELM QVADKILPFM DCTWRLLDEG YREGKHILFE GAQGALLDND FGTYPYVTSS
     NTVAGQACTG SGMGPGVIHY VLGIAKAYTT RVGEGPFPTE QINDIGEFLG TRGHEFGVVT
     GRKRRCGWFD AVLVRQMVAI CGVQGIALTK LDVLDGLDEI KICIGYELDG RKIDYLPSSM
     GAQARVKPIY ETLEGWKAKT AHTLRWEDLP VQAVKYIRYI EELINTKVAL LSTSPEREDT
     ILITDPFAN
//