ID PURA1_BURL3 Reviewed; 448 AA. AC Q39FS0; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 28-JAN-2026, entry version 114. DE RecName: Full=Adenylosuccinate synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AMPSase 1 {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AdSS 1 {ECO:0000255|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011}; DE AltName: Full=IMP--aspartate ligase 1 {ECO:0000255|HAMAP-Rule:MF_00011}; GN Name=purA1 {ECO:0000255|HAMAP-Rule:MF_00011}; GN OrderedLocusNames=Bcep18194_A5102; OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / OS R18194 / 383). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; OC Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. 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; CP000151; ABB08696.1; -; Genomic_DNA. DR RefSeq; WP_011352252.1; NC_007510.1. DR AlphaFoldDB; Q39FS0; -. DR SMR; Q39FS0; -. DR GeneID; 45094978; -. DR KEGG; bur:Bcep18194_A5102; -. DR PATRIC; fig|482957.22.peg.2039; -. DR HOGENOM; CLU_029848_0_0_4; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000002705; Chromosome 1. 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-UniRule. DR GO; GO:0046040; P:IMP metabolic process; IEA:TreeGrafter. DR CDD; cd03108; AdSS; 1. DR FunFam; 1.10.300.10:FF:000001; Adenylosuccinate synthetase; 1. DR FunFam; 3.90.170.10: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 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; NF002223; PRK01117.1; 1. 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; GTP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..448 FT /note="Adenylosuccinate synthetase 1" FT /id="PRO_0000224264" FT ACT_SITE 23 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT ACT_SITE 51 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 22..28 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 23..26 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 23 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 48..51 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 50..52 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 139 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 153 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 234 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 249 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 317..323 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 321 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 323 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 349..351 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 431..433 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" SQ SEQUENCE 448 AA; 48133 MW; 59ABC05C2C92CDBC CRC64; MSASAVNVTP GRNVVVVGTQ WGDEGKGKIV DWLTDHAQGV VRFQGGHNAG HTLIIGGKKT ILRLIPSGIM REGVACYIGN GVVLSPEALF KEIGELEEAG VNVRDRLFIS EATTLILPYH IAIDQAREAR KGAGKIGTTG RGIGPAYEDK VGRRALRVQD LFDAKTFADR LRENLDFHNF VLTQYLGGAA VDFQATLDTM LGYADRLKPM VADVSRRLYD ANNAGQNLLF EGAQGTLLDI DHGTYPFVTS SNCVAGAASA GAGVGPQKLN YILGITKAYC TRVGSGPFPS ELYDADNPQR QDQVGVTLAN VGKEFGSVTG RPRRTGWLDA AALRRSIQIN GVSGLCMTKL DVLDGLDEVK LCVGYKIDGK DADILPRGAA DVARCEPVYE TFAGWKESTV GIKTWEALPA NAQAYLTRVQ EVAGVPVDMV STGPDRDETI LLRHPFKV //