ID PURA_ANADF Reviewed; 431 AA. AC A7HDA9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 28-JAN-2026, entry version 93. 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}; GN OrderedLocusNames=Anae109_2504; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5; RX PubMed=25614562; DOI=10.1128/genomea.01449-14; RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C., RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J., RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A., RA Loeffler F.E., Fields M.W.; RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic, RT metal-reducing bacterium isolated from a contaminated subsurface RT environment."; RL Genome Announc. 3:0-0(2015). 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; CP000769; ABS26705.1; -; Genomic_DNA. DR RefSeq; WP_012097297.1; NC_009675.1. DR AlphaFoldDB; A7HDA9; -. DR SMR; A7HDA9; -. DR STRING; 404589.Anae109_2504; -. DR KEGG; afw:Anae109_2504; -. DR eggNOG; COG0104; Bacteria. DR HOGENOM; CLU_029848_0_0_7; -. DR OrthoDB; 9807553at2; -. DR UniPathway; UPA00075; UER00335. 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. FT CHAIN 1..431 FT /note="Adenylosuccinate synthetase" FT /id="PRO_1000000774" 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 BINDING 12..18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00011" FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00011" FT BINDING 40..42 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 130 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 144 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 225 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 240 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 300..306 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 304 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 306 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 332..334 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 414..416 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" SQ SEQUENCE 431 AA; 46656 MW; F3874DD987AAA924 CRC64; MPNVVVVGAQ WGDEGKGKIV DLLTEHADVV VRFQGGNNAG HTLVVNGEKT VLHLIPAGIL HPGKSCVIGN GVVFDPEVFV MEVDRLKSRN ALADDSQLVV SLDAHVIMPW HKAIDIAREQ AMGAGKIGTT GRGIGPTYED KVARRGLRIR DLLDAARLER KVKERLPAAR EELSRLGATP ELDEAAIVAR YSELGRRVAR YAADVSLWLH RALQNGKQLL FEGAQGTMLD VDHGTYPFVT SSNTVAGNAV VGCGLGPTAV DYVLGISKAY STRVGGGPYP SELKDETGER LRKIGGEFGA TTGRPRRTGW LDALALRYAA RVNGLHGIAM TKLDVLAGFE TVKIAVGYRV DGKVLDEMPS DPELLERAEA VYEELPGWTE KLEDLRSWDD LPPRARAYVK RVEQLVGVPV VGLSVGADRG QTILLENPFR A //