ID PURA_AGGAC Reviewed; 259 AA. AC P96771; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 02-SEP-2026, entry version 112. 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}; DE Flags: Fragment; GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; OS Aggregatibacter actinomycetemcomitans (Actinobacillus OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=714; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CU1000; RX PubMed=9631542; DOI=10.1111/j.1574-6968.1998.tb13022.x; RA Kaplan J.B., Fine D.H.; RT "Codon usage in Actinobacillus actinomycetemcomitans."; RL FEMS Microbiol. Lett. 163:31-36(1998). 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=IMP + L-aspartate + GTP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP CC + phosphate + 2 H(+); Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC 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; U89525; AAC46412.1; -; Genomic_DNA. DR AlphaFoldDB; P96771; -. DR SMR; P96771; -. DR STRING; 714.ACT75_02600; -. DR PaxDb; 714-ACT75_02600; -. DR eggNOG; COG0104; Bacteria. DR UniPathway; UPA00075; UER00335. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046040; P:IMP metabolic process; IEA:TreeGrafter. DR FunFam; 1.10.300.10:FF:000001; Adenylosuccinate synthetase; 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 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; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027417; P-loop_NTPase. 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; GTP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis. FT CHAIN <1..259 FT /note="Adenylosuccinate synthetase" FT /id="PRO_0000095139" FT ACT_SITE 4 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT ACT_SITE 32 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 3..9 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 4..7 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:0000255|HAMAP-Rule:MF_00011" FT BINDING 4 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 31..33 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 31 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 120 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:0000255|HAMAP-Rule:MF_00011" FT BINDING 134 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 215 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:0000255|HAMAP-Rule:MF_00011" FT BINDING 230 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:0000255|HAMAP-Rule:MF_00011" FT NON_TER 1 SQ SEQUENCE 259 AA; 28479 MW; E64198443875D6C6 CRC64; QWGDEGKGKI VDLLTDRVKY VVRYQGGRGA GHTLILNGEK TVLRLIPSGI LRDNVTCLIG NGVVLSPAAL MQEMSELENR GVNVRDRLLI SEACPLILPY HVAMDHAREA RWAKRPIRAT GRGIGPAYED KVARRGLRVG DLFDRAAFAE KLKNILDYYN FQLVNYYKVE PVDYQKTLDD VFAVADIITG MVADITTILD TARKNGDNIL FEGAQGTMLD IDHGTYPYVT SSNTAGGVAS GSGFGPRNLD YVLGIIKAY //