ID A0A3N4HER3_ASCIM Unreviewed; 439 AA. AC A0A3N4HER3; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 03-AUG-2022, entry version 10. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520}; DE Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_03125}; DE Short=AdSS {ECO:0000256|HAMAP-Rule:MF_03125}; DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520}; DE AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_03125}; GN ORFNames=BJ508DRAFT_419643 {ECO:0000313|EMBL:RPA72087.1}; OS Ascobolus immersus RN42. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes; OC Pezizales; Ascobolaceae; Ascobolus. OX NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA72087.1, ECO:0000313|Proteomes:UP000275078}; RN [1] {ECO:0000313|EMBL:RPA72087.1, ECO:0000313|Proteomes:UP000275078} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RN42 {ECO:0000313|EMBL:RPA72087.1, RC ECO:0000313|Proteomes:UP000275078}; RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4; RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A., RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M., RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B., RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A., RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C., RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L., RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S., RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M., RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.; RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal RT truffle lifestyle."; RL Nat. Ecol. Evol. 2:1956-1965(2018). CC -!- FUNCTION: Plays an important role in the de novo pathway and in the CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first CC commited step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP- CC Rule:MF_03125}. CC -!- FUNCTION: Plays an important role in the de novo pathway and in the CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first CC committed step in the biosynthesis of AMP from IMP. CC {ECO:0000256|ARBA:ARBA00003779}. CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. {ECO:0000256|RuleBase:RU000520}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2- CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03125, ECO:0000256|RuleBase:RU000520}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03125}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03125}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125, CC ECO:0000256|RuleBase:RU000520}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_03125}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520}. 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; ML119880; RPA72087.1; -; Genomic_DNA. DR STRING; 1160509.A0A3N4HER3; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000275078; Unassembled WGS sequence. 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-UniPathway. DR CDD; cd03108; AdSS; 1. DR Gene3D; 1.10.300.10; -; 1. DR Gene3D; 3.40.440.10; -; 1. DR Gene3D; 3.90.170.10; -; 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 PANTHER; PTHR11846; PTHR11846; 1. DR Pfam; PF00709; Adenylsucc_synt; 1. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00184; purA; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_03125}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03125}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03125}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03125}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03125}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_03125}; Reference proteome {ECO:0000313|Proteomes:UP000275078}. FT REGION 12..15 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT REGION 37..40 FT /note="IMP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT REGION 301..307 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT ACT_SITE 12 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT ACT_SITE 40 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT ACT_SITE 140 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134" FT BINDING 11..17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 12 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 39..41 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 129 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 143 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 226 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 241 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 305 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 307 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 333..335 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 416..418 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" SQ SEQUENCE 439 AA; 48095 MW; 0653FC09A4FE32C0 CRC64; MTTIILGAQF GDEGKGKLVD VLCRSADICA RSAGGSNAGH TVVANGITYD FHLLPSGLVH EQCTNVIGSG VVAHIPSFFD ELEAAQSKGL NTEGRIKISN RAHIVLDLHR TVDGLEEEEL GKNKSIGTTK RGIGPTYANK ASRNGLRIAD LYTWDTFEEK FRRLVAGYRK RFGHLEGFSY DDAAVEAELV RYKEYAERLK PFVVDAVTYM SKATASNKRI IVEGANALLL DIDYGTYPFV TSSNASLGGC ITGLALNPLA IKEIIGVVKA YTTRVGGGPF PTELFDEVGE QIATIGHEIG VTTKRKRRCG WLDLVLVKYS HSVNHYTSIN LTKLDILDAF DEIKVCEAYE VDGQIIEDFP ADAETLAKVK PVYKSYPGWK SSPIMNTTSI KQWSQTTVDY VRHIEEFLGV KISSVGVGPK REHLIEAEVA GQSVLDNKN //