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 10-AUG-2010, 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=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]. 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 (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; -. DR GeneID; 7666909; -. DR GenomeReviews; CP001357_GR; BHWA1_01817. DR KEGG; bhy:BHWA1_01817; -. DR OMA; YVLGIIK; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:EC. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00011; Adenylosucc_synth; 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 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 1 427 Adenylosuccinate synthetase. FT /FTId=PRO_1000116455. FT NP_BIND 12 18 GTP (Potential). FT ACT_SITE 139 139 By similarity. FT ACT_SITE 146 146 By similarity. FT METAL 13 13 Magnesium (By similarity). FT METAL 40 40 Magnesium; via carbonyl oxygen (By FT 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 //