ID F0NPQ3_SULIH Unreviewed; 406 AA. AC F0NPQ3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-SEP-2021, entry version 54. DE RecName: Full=Argininosuccinate synthase {ECO:0000256|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000256|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00005}; GN Name=argG {ECO:0000256|HAMAP-Rule:MF_00005}; GN OrderedLocusNames=SiH_1462 {ECO:0000313|EMBL:ADX82810.1}; OS Sulfolobus islandicus (strain HVE10/4). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX82810.1, ECO:0000313|Proteomes:UP000006395}; RN [1] {ECO:0000313|EMBL:ADX82810.1, ECO:0000313|Proteomes:UP000006395} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX82810.1, RC ECO:0000313|Proteomes:UP000006395}; RX PubMed=21278296; DOI=10.1128/JB.01487-10; RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S., RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q., RA Huang L., Garrett R.A.; RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model RT organisms for genetic and virus-host interaction studies."; RL J. Bacteriol. 193:1672-1680(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L- CC arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743, CC ChEBI:CHEBI:456215; EC=6.3.4.5; CC Evidence={ECO:0000256|ARBA:ARBA00001891, ECO:0000256|HAMAP- CC Rule:MF_00005}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 2/3. CC {ECO:0000256|ARBA:ARBA00004967, ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00005}. 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; CP002426; ADX82810.1; -; Genomic_DNA. DR RefSeq; WP_014512699.1; NC_017275.1. DR EnsemblBacteria; ADX82810; ADX82810; SiH_1462. DR GeneID; 12415535; -. DR KEGG; sih:SiH_1462; -. DR HOGENOM; CLU_032784_4_2_2; -. DR OMA; QCEVVTF; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000006395; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01999; Argininosuccinate_Synthase; 1. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.1260.10; -; 1. DR HAMAP; MF_00005; Arg_succ_synth_type1; 1. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR023434; Arginosuc_synth_type_1_subfam. DR InterPro; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR11587; PTHR11587; 1. DR Pfam; PF00764; Arginosuc_synth; 1. DR SUPFAM; SSF69864; SSF69864; 1. DR TIGRFAMs; TIGR00032; argG; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00005}; KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP- KW Rule:MF_00005}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00005}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00005}. FT NP_BIND 21..29 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 99 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 129 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 131 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 135 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 135 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 136 FT /note="Aspartate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 139 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 186 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 195 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 268 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 280 FT /note="Citrulline" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" SQ SEQUENCE 406 AA; 46255 MW; FEAF401F66491672 CRC64; MISIVFKLLL YPFCEMKIVL AYSGGLDTTV SIRWLKETFK AEVITVTVDV GQKDDFKKIE ERAYIAGASK HYTIDVIKEF ANNYISYAIK LNGLYEGVYP LSTALARPLI AEKVVEVAKK EKADAVAHGS TSKGNDQVRF DLTVKALYPD VKIIAPARIW SMTREDEIKY AKEKGIPIKV ESSKYSIDEN LWGRSIEGDI ISDPSVEVTE DAFEWTKQIA NNKEIISIEF SNGVPTAVDG EQMELHKLIG LLNLKFGNHG FGRVEHIENR VVGFKSREVY EVPAALGLIY SHIDLEKTIY TPTELRFKKY VDQLWSDLVY QGLWFEPLRE TLHKIADEMN KWIAGEVRVE VNNGSFRILG RKSDYSPYSE KLASYNKGWY PSDEMARGFI EIWGMHSLIA RRVRGL //