ID B9JA15_RHIR8 Unreviewed; 407 AA. AC B9JA15; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Argininosuccinate synthase {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916, ECO:0000256|HAMAP-Rule:MF_00005}; GN Name=argG2 {ECO:0000313|EMBL:ACM25633.1}; GN Synonyms=argG {ECO:0000256|HAMAP-Rule:MF_00005}; GN OrderedLocusNames=Arad_1099 {ECO:0000313|EMBL:ACM25633.1}; OS Rhizobium rhizogenes (strain K84 / ATCC BAA-868) (Agrobacterium OS radiobacter). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=311403 {ECO:0000313|EMBL:ACM25633.1, ECO:0000313|Proteomes:UP000001600}; RN [1] {ECO:0000313|EMBL:ACM25633.1, ECO:0000313|Proteomes:UP000001600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K84 / ATCC BAA-868 {ECO:0000313|Proteomes:UP000001600}; RX PubMed=19251847; DOI=10.1128/JB.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L., RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A., RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M., RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N., RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). 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; Evidence={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 --------------------------------------------------------------------------- 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; CP000628; ACM25633.1; -; Genomic_DNA. DR AlphaFoldDB; B9JA15; -. DR STRING; 311403.Arad_1099; -. DR KEGG; ara:Arad_1099; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_5; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000001600; Chromosome 1. 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; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00005; Arg_succ_synth_type1; 1. DR InterPro; IPR048268; Arginosuc_syn_C. DR InterPro; IPR048267; Arginosuc_syn_N. 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 NCBIfam; TIGR00032; argG; 1. DR PANTHER; PTHR11587; ARGININOSUCCINATE SYNTHASE; 1. DR PANTHER; PTHR11587:SF2; ARGININOSUCCINATE SYNTHASE; 1. DR Pfam; PF20979; Arginosuc_syn_C; 1. DR Pfam; PF00764; Arginosuc_synth; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 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 DOMAIN 7..168 FT /note="Arginosuccinate synthase-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00764" FT DOMAIN 179..397 FT /note="Arginosuccinate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF20979" FT BINDING 11..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 89 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 94 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 121 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 126 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 129 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 180 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 189 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 265 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 277 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" SQ SEQUENCE 407 AA; 45095 MW; 281AA834D83E220A CRC64; MIKDIKKIVL SYSGGLDTSI ILKWLQETYK CEVVTFTADL GQGEELEPAR AKAEMLAIKD IRIVDVREEF VRDFVFPMFR ANTVYEGQYL LGSSIARPLI AKHLVRIAQD VGADAISHGA TGKGNDQVRF ELTVNALDPS IKVIAPWREW NIQSRTQLID YAERNQIPVP TDKRGEAPFS IDANLLHTSS EGKVLEDPAD IAPDYVYQRT VDPVDAPNVP EIITIGFEKG DAVSLNGVKL SPATLLTRLN ELGGRHGVGR IDLVENRFVG MKSRGVYETP GGTILLAAHR GIESITLDRG AAHLKDEIMP RYAELIYNGF WYAPEREMLQ ALIDRSQTHV AGEVTVKLHK GSASVIARNS SNSLYSMDLV TFEEGSGSYD HHDAEGFIKL NGLRLKTLAA RNKRLGR //