ID A0A3N4HER3_ASCIM Unreviewed; 439 AA. AC A0A3N4HER3; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 19-JAN-2022, entry version 9. 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 NP_BIND 11..17 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT NP_BIND 39..41 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT NP_BIND 333..335 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT NP_BIND 416..418 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" 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 METAL 12 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT METAL 39 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 129 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 143 FT /note="IMP; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 226 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 241 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 305 FT /note="IMP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125" FT BINDING 307 FT /note="GTP" 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 //