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 12-AUG-2020, entry version 67. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011}; DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011}; GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; OrderedLocusNames=BHWA1_01817; OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1). OC Bacteria; Spirochaetes; Brachyspirales; 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 large RT 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. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2- CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00011}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00011}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00011}. 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; WP_012671320.1; NC_012225.1. DR SMR; C0R2E2; -. DR STRING; 565034.BHWA1_01817; -. DR EnsemblBacteria; ACN84280; ACN84280; BHWA1_01817. DR KEGG; bhy:BHWA1_01817; -. DR eggNOG; COG0104; Bacteria. DR HOGENOM; CLU_029848_0_0_12; -. DR KO; K01939; -. DR OMA; FHHAKPI; -. DR BioCyc; BHYO565034:G1GUM-1774-MONOMER; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000001803; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd03108; AdSS; 1. DR Gene3D; 1.10.300.10; -; 1. DR Gene3D; 3.40.440.10; -; 1. DR Gene3D; 3.90.170.10; -; 1. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS. DR InterPro; IPR042109; Adenylosuccinate_synth_dom1. DR InterPro; IPR042110; Adenylosuccinate_synth_dom2. DR InterPro; IPR042111; Adenylosuccinate_synth_dom3. 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 Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis. FT CHAIN 1..427 FT /note="Adenylosuccinate synthetase" FT /id="PRO_1000116455" FT NP_BIND 12..18 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT NP_BIND 40..42 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT NP_BIND 330..332 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT NP_BIND 412..414 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT REGION 13..16 FT /note="IMP binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT REGION 38..41 FT /note="IMP binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT REGION 298..304 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT ACT_SITE 13 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT ACT_SITE 41 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT METAL 13 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT METAL 40 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 128 FT /note="IMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 142 FT /note="IMP; shared with dimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 223 FT /note="IMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 238 FT /note="IMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 302 FT /note="IMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 304 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" 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 //