ID   PURA_AZOSE              Reviewed;         436 AA.
AC   Q5P7C4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 38.
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=AZOSEA06640; ORFNames=ebA1249;
OS   Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI06787.1; -; Genomic_DNA.
DR   RefSeq; YP_157688.1; -.
DR   GeneID; 3181837; -.
DR   GenomeReviews; CR555306_GR; AZOSEA06640.
DR   KEGG; eba:ebA1249; -.
DR   NMPDR; fig|76114.4.peg.1977; -.
DR   HOGENOM; Q5P7C4; -.
DR   OMA; Q5P7C4; YVLGIIK.
DR   BioCyc; ASP76114:EBA1249-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    436       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000224249.
FT   NP_BIND      13     19       GTP (Potential).
FT   ACT_SITE    142    142       By similarity.
FT   ACT_SITE    149    149       By similarity.
FT   METAL        14     14       Magnesium (By similarity).
FT   METAL        41     41       Magnesium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   436 AA;  47067 MW;  64CAFD6245C296FD CRC64;
     MAKNVVVVGT QWGDEGKGKI VDWLTDHARG VVRFQGGHNA GHTLVIGANE YKLNLVPSGI
     VREGVACYIG NGVVLDAHHL LSEIRTLEAG GIRVRDRLRI SPGCPLILGY HAALDRAREA
     AKSAGDKIGT TGKGIGPTYE DKVARRALRV YDLFDRERFA AKLRANLDYH NFVLTQHLGA
     EAVEFGSVFE QAMADAEEIR PMVADVSAEL YAVNKSGGSL LFEGAQGTLL DIDHGTYPFV
     TSSNCVAGQA AAGSGVGPGR LHYVLGITKA YCTRVGGGPF PTELDIETAD TPGQQMSSKG
     REFGTVTGRK RRCGWLDLGA LKRSIIINGV TGLCITKLDV LDGLSELKLC TGYMLDGRRI
     DLLPMGSEEV TRCEPIFETM AGWSGTTFGA QSWEALPQEA RAYLHRIEEI CEIAIDVIST
     GPERDETILR RHPFGA
//