ID A0A6G9EY47_9ACTN Unreviewed; 427 AA. AC A0A6G9EY47; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 24-JAN-2024, entry version 14. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}; DE Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011}; DE Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}; DE AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011}; GN Name=purA {ECO:0000256|HAMAP-Rule:MF_00011}; GN ORFNames=EZV63_18925 {ECO:0000313|EMBL:QIP71671.1}; OS Streptomyces sp. VN1. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1821625 {ECO:0000313|EMBL:QIP71671.1, ECO:0000313|Proteomes:UP000502084}; RN [1] {ECO:0000313|EMBL:QIP71671.1, ECO:0000313|Proteomes:UP000502084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VN1 {ECO:0000313|EMBL:QIP71671.1, RC ECO:0000313|Proteomes:UP000502084}; RX PubMed=32019976; RA Nguyen H.T., Pokhrel A.R., Nguyen C.T., Pham V.T.T., Dhakal D., Lim H.N., RA Jung H.J., Kim T.S., Yamaguchi T., Sohng J.K.; RT "Streptomyces sp. VN1, a producer of diverse metabolites including non- RT natural furan-type anticancer compound."; RL Sci. Rep. 10:0-1756(2020). 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:0000256|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:0000256|HAMAP- CC Rule:MF_00011, ECO:0000256|RuleBase:RU000520}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00011}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00011}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011, CC ECO:0000256|RuleBase:RU000520}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_00011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}. 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; CP036534; QIP71671.1; -; Genomic_DNA. DR RefSeq; WP_031043628.1; NZ_CP036534.1. DR AlphaFoldDB; A0A6G9EY47; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000502084; 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; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1. DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1. DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 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 NCBIfam; TIGR00184; purA; 1. DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1. DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00011}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00011}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00011}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00011}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00011}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_00011}. FT ACT_SITE 13 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT ACT_SITE 41 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT ACT_SITE 139 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134" FT BINDING 12..18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 13..16 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 38..41 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 40..42 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 128 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 142 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 223 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 238 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 298..304 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 302 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 304 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 330..332 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" FT BINDING 412..414 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00011" SQ SEQUENCE 427 AA; 45910 MW; 57CD5B2D39CD6AE1 CRC64; MPALVLLGAQ WGDEGKGKAT DLLGGSVDYV VRYQGGNNAG HTVVVGDQKY ALHLLPSGIL SPGCTPVIGN GVVVDPSVLF SELSGLNERG VDTSKLLISG NAHIITPYNV TVDKVTERFL GKRKIGTTGR GIGPTYADKI NRVGIRVQDL YDESILTQKV EAALDVKNQM LTKLYNRRAI ATGQVVEELM GYADKLAPYV ADTVLVLNEA LDDDKVVLFE GGQGTLLDID HGTYPFVTSS NPTAGGACTG AGVGPTKISR VIGILKAYTT RVGAGPFPTE LFDEDGEALR RIGGERGVTT GRDRRCGWFD AVIARYATRV NGLTDFFLTK LDVLTGWEEI PVCVAYEIDG RRVEELPYSQ SDFHHAKPVY ETLPGWSEDI TKAKSFSDLP KNAQAYVRAL EEMSGAPISA IGVGPGRDET IEINSFL //