ID PURA1_METAC Reviewed; 424 AA. AC Q8TPJ2; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 04-NOV-2026, entry version 118. 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=MA_1919; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., RA Zinder S.H., Lander E., Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and RT physiological diversity."; RL Genome Res. 12:532-542(2002). 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; AE010299; AAM05323.1; -; Genomic_DNA. DR RefSeq; WP_011021916.1; NC_003552.1. DR AlphaFoldDB; Q8TPJ2; -. DR SMR; Q8TPJ2; -. DR FunCoup; Q8TPJ2; 290. DR STRING; 188937.MA_1919; -. DR EnsemblBacteria; AAM05323; AAM05323; MA_1919. DR GeneID; 1473808; -. DR KEGG; mac:MA_1919; -. DR HOGENOM; CLU_029848_0_0_2; -. DR InParanoid; Q8TPJ2; -. DR OMA; AALLXTY; -. DR OrthoDB; 372247at2157; -. DR PhylomeDB; Q8TPJ2; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000002487; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central. 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; 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. PE 3: Inferred from homology; KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..424 FT /note="Adenylosuccinate synthetase 1" FT /id="PRO_0000095269" 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 127 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 141 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 236 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 413..415 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" SQ SEQUENCE 424 AA; 46812 MW; AFE917A824D8EB35 CRC64; MSVTVIVGAQ CGDEGKGKMV DLIAQDYDLV IRFQGGDNAG HTVVNQYGTF KMHLIPCGIF NQNAISLVGT GMVVNPDELQ KEMKQITSAG MSVDNLKIST RANILMPYHR DLDELNEQSG GMSIGTTKRG IGPAYAGRAT RTNIRFGDLA HQDYLKSHFE KVLPAINHQL SFFGAAQYTV DQLCEYCSNW YKLYNEHIVD AFTLIHNMMK ENKRILFEGQ LGVMKDIDLG IYPFVTSSNP IAAYAAVSSG IPARSITSVI GVAKAFSSQV GDGPFPTEVL DNCIVSLRGT GKNIDDEFGA RTGRPRRLGW LDIPVLRYAH TINGFDTLAI CKLDKMDSLP EIKICTSYRY QDQILSVFPD TEILGQVKAE YETLPGWECT TRGVNSFDDL PENAKSYIKR IEELVGVPVK YIGVGPARSD VIIR //