ID F0NPQ3_SULIH Unreviewed; 406 AA. AC F0NPQ3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 13-NOV-2019, entry version 47. 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(+); CC Xref=Rhea:RHEA:10932, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, CC ChEBI:CHEBI:57743, ChEBI:CHEBI:456215; EC=6.3.4.5; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00005}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC {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 CC 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 EnsemblBacteria; ADX82810; ADX82810; SiH_1462. DR KEGG; sih:SiH_1462; -. DR KO; K01940; -. DR OMA; QCEVVTF; -. DR BioCyc; SISL930943:G1GRJ-1737-MONOMER; -. 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|HAMAP-Rule:MF_00005}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00005}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00005}; KW Complete proteome {ECO:0000313|Proteomes:UP000006395}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00005}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00005}. FT NP_BIND 21 29 ATP. {ECO:0000256|HAMAP-Rule:MF_00005}. FT BINDING 99 99 Citrulline. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 129 129 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00005}. FT BINDING 131 131 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 135 135 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 135 135 Citrulline. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 136 136 Aspartate. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 139 139 Citrulline. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 186 186 Citrulline. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 195 195 Citrulline. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 268 268 Citrulline. {ECO:0000256|HAMAP-Rule: FT MF_00005}. FT BINDING 280 280 Citrulline. {ECO:0000256|HAMAP-Rule: FT 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 //