ID A0A3N4HER3_ASCIM Unreviewed; 439 AA. AC A0A3N4HER3; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 10-APR-2019, entry version 2. 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}; RN [1] {ECO:0000313|EMBL:RPA72087.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RN42 {ECO:0000313|EMBL:RPA72087.1}; 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., RA Dockter R.B., Fauchery L., Guy J., Iotti M., Le Tacon F., RA Lindquist E.A., Lipzen A., Malagnac F., Mello A., Molinier V., RA Miyauchi S., Poulain J., Riccioni C., Rubini A., Sitrit Y., RA Splivallo R., Traeger S., Wang M., Zifcakova L., Wipf D., RA Zambonelli A., Paolocci F., Nowrousian M., Ottonello S., Baldrian P., RA Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M., Wincker P., RA 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 CC the salvage pathway of purine nucleotide biosynthesis. Catalyzes CC the first commited step in the biosynthesis of AMP from IMP. CC {ECO:0000256|HAMAP-Rule:MF_03125}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03125}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03125}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125, CC ECO:0000256|RuleBase:RU000520}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-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 UniPathway; UPA00075; UER00335. DR CDD; cd03108; AdSS; 1. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS. 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|HAMAP-Rule:MF_03125, KW ECO:0000256|RuleBase:RU000520}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_03125, KW ECO:0000256|RuleBase:RU000520}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03125, KW ECO:0000256|RuleBase:RU000520}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03125, KW ECO:0000256|RuleBase:RU000520}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03125, KW ECO:0000256|RuleBase:RU000520}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03125, KW ECO:0000256|RuleBase:RU000520}. FT NP_BIND 11 17 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT NP_BIND 39 41 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT NP_BIND 333 335 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT NP_BIND 416 418 GTP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT REGION 12 15 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_03125}. FT REGION 37 40 IMP binding. {ECO:0000256|HAMAP-Rule: FT MF_03125}. FT REGION 301 307 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03125}. FT ACT_SITE 12 12 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03125}. FT ACT_SITE 40 40 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_03125}. FT ACT_SITE 140 140 {ECO:0000256|PROSITE-ProRule:PRU10134}. FT METAL 12 12 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_03125}. FT METAL 39 39 Magnesium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03125}. FT BINDING 129 129 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT BINDING 143 143 IMP; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_03125}. FT BINDING 226 226 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT BINDING 241 241 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT BINDING 305 305 IMP. {ECO:0000256|HAMAP-Rule:MF_03125}. FT BINDING 307 307 GTP. {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 //