ID   PURA_BACTN              Reviewed;         423 AA.
AC   Q8A6N4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 46.
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_1843;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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; AE015928; AAO76950.1; -; Genomic_DNA.
DR   RefSeq; NP_810756.1; -.
DR   HSSP; P12283; 1ADE.
DR   GeneID; 1075166; -.
DR   GenomeReviews; AE015928_GR; BT_1843.
DR   KEGG; bth:BT_1843; -.
DR   NMPDR; fig|226186.1.peg.1843; -.
DR   HOGENOM; Q8A6N4; -.
DR   OMA; Q8A6N4; IPVCVAY.
DR   BioCyc; BTHE226186:BT_1843-MON; -.
DR   BRENDA; 6.3.4.4; 21018.
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    423       Adenylosuccinate synthetase.
FT                                /FTId=PRO_0000095147.
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   423 AA;  46789 MW;  1569243D88FB2FDB CRC64;
     MKVDVLLGLQ WGDEGKGKVV DVLTPKYDVV ARFQGGPNAG HTLEFEGQKY VLRSIPSGIF
     QGDKVNIIGN GVVLDPALFK AEAEALEASG HPLKERLHIS KKAHLILPTH RILDAAYEAA
     KGDAKVGTTG KGIGPTYTDK VSRNGVRVGD ILHNFEQKYG AAKARHEQIL KSLNYEYDLT
     ELEKAWMEGI EYLKQFHFVD SEHEVNNYLK DGKSVLCEGA QGTMLDIDFG SYPFVTSSNT
     VCAGACTGLG VAPNRIGEVF GIFKAYCTRV GAGPFPTELF DETGDKMCTL GHEFGSVTGR
     KRRCGWIDLV ALKYSVMING VTKLIMMKSD VLDTFDTIKA CVAYKVDGEE IDYFPYDITE
     GVEPVYAELP GWKTDMTKMQ SEDEFPEEFN AYLTFLEEQL GVEIKIVSVG PDRAQTIERY
     TEE
//