ID PURA_BRAHW Reviewed; 427 AA. AC C0R2E2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 16-OCT-2013, entry version 31. DE RecName: Full=Adenylosuccinate synthetase; DE Short=AMPSase; DE Short=AdSS; DE EC=6.3.4.4; DE AltName: Full=IMP--aspartate ligase; GN Name=purA; OrderedLocusNames=BHWA1_01817; OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1). OC Bacteria; Spirochaetes; Spirochaetales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=565034; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49526 / WA1; RX PubMed=19262690; DOI=10.1371/journal.pone.0004641; RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P., RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A., RA Barrero R., Phillips N.D., Hampson D.J.; RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira RT hyodysenteriae reveals adaptations to its lifestyle in the porcine RT large intestine."; RL PLoS ONE 4:E4641-E4641(2009). CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. Catalyzes the first committed step in the CC biosynthesis of AMP from IMP (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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001357; ACN84280.1; -; Genomic_DNA. DR RefSeq; YP_002721984.1; NC_012225.1. DR STRING; 565034.BHWA1_01817; -. DR EnsemblBacteria; ACN84280; ACN84280; BHWA1_01817. DR GeneID; 7666909; -. DR KEGG; bhy:BHWA1_01817; -. DR PATRIC; 21181691; VBIBraHyo62857_1769. DR eggNOG; COG0104; -. DR HOGENOM; HOG000260959; -. DR KO; K01939; -. DR OMA; DYVVRYQ; -. DR ProtClustDB; CLSK2810299; -. DR BioCyc; BHYO565034:GJI7-1805-MONOMER; -. DR UniPathway; UPA00075; UER00335. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00011; Adenylosucc_synth; 1; -. DR InterPro; IPR018220; Adenylosuccinate_synthase_AS. DR InterPro; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11846; PTHR11846; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; SSF52540; 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 1 427 Adenylosuccinate synthetase. FT /FTId=PRO_1000116455. FT NP_BIND 12 18 GTP (By similarity). FT NP_BIND 40 42 GTP (By similarity). FT NP_BIND 330 332 GTP (By similarity). FT NP_BIND 412 414 GTP (By similarity). FT REGION 13 16 IMP binding (By similarity). FT REGION 38 41 IMP binding (By similarity). FT REGION 298 304 Substrate binding (By similarity). FT ACT_SITE 13 13 Proton acceptor (By similarity). FT ACT_SITE 41 41 Proton donor (By similarity). FT METAL 13 13 Magnesium (By similarity). FT METAL 40 40 Magnesium; via carbonyl oxygen (By FT similarity). FT BINDING 128 128 IMP (By similarity). FT BINDING 142 142 IMP; shared with dimeric partner (By FT similarity). FT BINDING 223 223 IMP (By similarity). FT BINDING 238 238 IMP (By similarity). FT BINDING 302 302 IMP (By similarity). FT BINDING 304 304 GTP (By similarity). SQ SEQUENCE 427 AA; 47541 MW; 285013BAE54B3940 CRC64; MASVIIVGTQ WGDEGKGKIV DYLAENCEYV VRSQGGSNAG HTVVVDNIKY KLRLLPSGIL HKDKVCVIGN GVVIEPKVFL SEIDSLIEKK VNISNLKISD RAHVLMPYHK ILDELQEEDL GENKLGTTKN GIGPCYMDKS SRLGIRIVDL MNKETFAKKL KFNVELKNKL LKKLYNHDGV NYDELLKEYL GYAEKLRPFV ADTTTILNKA IKEKKNILFE GAQATMLDLD HGTYPFVTSS YPAAGGACTG SGVGPRKIDN VIGVVKAYAT RVGEGPFPSE LFDDVGQFIR DKGGEYGTVT GRARRCGWLD ACVVKYASYV NGLDSIAITR LDILDELDKL KICVAYKYNS EILEGYPADL DILSKVEPVY EEFEGWKTST RDIREYDKLP ENAKKYLKRL SEVIETDISI VSVGAGRDET IIVKKIF //