ID PURA_PYRHO Reviewed; 339 AA. AC O58187; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 10-JUN-2026, entry version 152. 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}; OrderedLocusNames=PH0438; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Methanobacteriati; Methanobacteriota; Thermococci; Thermococcales; OC Thermococcaceae; Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of hypothetical adenylosuccinate synthetase, PH0438 from RT Pyrococcus horikoshii OT3."; RL Submitted (MAY-2006) to the PDB data bank. 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; BA000001; BAA29524.1; -; Genomic_DNA. DR PIR; G71154; G71154. DR RefSeq; WP_010884548.1; NC_000961.1. DR PDB; 2D7U; X-ray; 2.50 A; A=1-339. DR PDB; 5K7X; X-ray; 2.80 A; A/B/C/D/E/F=1-339. DR AlphaFoldDB; O58187; -. DR SMR; O58187; -. DR STRING; 70601.gene:9377369; -. DR EnsemblBacteria; BAA29524; BAA29524; BAA29524. DR GeneID; 1444335; -. DR KEGG; pho:PH0438; -. DR eggNOG; arCOG04387; Archaea. DR OrthoDB; 372247at2157; -. DR BRENDA; 6.3.4.4; 5244. DR UniPathway; UPA00075; UER00335. DR EvolutionaryTrace; O58187; -. DR Proteomes; UP000000752; 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-UniRule. DR GO; GO:0046040; P:IMP metabolic process; IEA:TreeGrafter. DR CDD; cd03108; AdSS; 1. DR FunFam; 3.40.440.10:FF:000005; Adenylosuccinate synthetase; 1. DR FunFam; 3.40.440.10:FF:000007; Adenylosuccinate synthetase; 1. DR FunFam; 3.90.170.10:FF:000002; Adenylosuccinate synthetase; 1. DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 2. 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; 2. 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; NF003295; PRK04293.1; 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 PDBsum; 2D7U; -. DR PDBsum; 5K7X; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..339 FT /note="Adenylosuccinate synthetase" FT /id="PRO_0000095277" FT ACT_SITE 13 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT ACT_SITE 43 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 40..43 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 42..44 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 42 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 179 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 194 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 252..258 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 256 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 258 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 284..286 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT BINDING 324..326 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00011" FT STRAND 4..12 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 50..57 FT /evidence="ECO:0007829|PDB:2D7U" FT TURN 59..62 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 64..70 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 118..124 FT /evidence="ECO:0007829|PDB:5K7X" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:5K7X" FT HELIX 131..138 FT /evidence="ECO:0007829|PDB:2D7U" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 159..168 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 173..180 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:2D7U" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 200..207 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 216..224 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 239..244 FT /evidence="ECO:0007829|PDB:2D7U" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 265..274 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 278..283 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:2D7U" FT HELIX 303..316 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 320..324 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 326..330 FT /evidence="ECO:0007829|PDB:2D7U" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:2D7U" SQ SEQUENCE 339 AA; 37232 MW; ADA2FB1D07CCF3D0 CRC64; MPSVIVVGGQ WGDEGKGSIV AYLSLHDEPE IIARGGVGTN AGHSVVINGK KYAVRQIPTG FMQTKARLLI GAGVLVDPEV FFHELEQLKD FNVKDRVGID YRCAIIEEKH KQLDRTNGYL HGKIGTTGSG CGPANADRVM RKAKQAKDVK ELEPYLTDVA QEINDALDEG SLVLVEGTQG FGLSLYYGTY PYVTSKDVTA SSVAADVGIG PTRVDEVIVV FKSFPTRVGA GPFPTEMPME EADRLGLVEY GTVTGRRRRV GWFDFEMARY SARINGATML AVTMLDKYDK EAFGVTDYDK LPRKAKEFIE EIEERVGVPV GLIKTGPELE HIIDRRDTI //