ID ASSY_RHOOB Reviewed; 399 AA. AC C1ASZ6; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 04-NOV-2026, entry version 98. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00005}; GN OrderedLocusNames=ROP_06810; OS Rhodococcus opacus (strain B4). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Nocardiaceae; Rhodococcus. OX NCBI_TaxID=632772; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus erythropolis RT PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-citrulline + L-aspartate + ATP = 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:0000255|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. {ECO:0000255|HAMAP- CC Rule:MF_00005}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 CC subfamily. {ECO:0000255|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; AP011115; BAH48928.1; -; Genomic_DNA. DR RefSeq; WP_009473614.1; NC_012522.1. DR AlphaFoldDB; C1ASZ6; -. DR SMR; C1ASZ6; -. DR STRING; 632772.ROP_06810; -. DR KEGG; rop:ROP_06810; -. DR PATRIC; fig|632772.20.peg.742; -. DR HOGENOM; CLU_032784_4_2_11; -. DR OMA; AACFQKM; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. 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:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0000050; P:urea cycle; IEA:TreeGrafter. DR CDD; cd01999; ASS; 1. DR FunFam; 3.40.50.620:FF:000038; Argininosuccinate synthase; 1. DR FunFam; 3.90.1260.10:FF:000007; 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 Gene3D; 1.20.5.470; Single helix bin; 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 NCBIfam; NF001770; PRK00509.1; 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; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding. FT CHAIN 1..399 FT /note="Argininosuccinate synthase" FT /id="PRO_1000116289" FT BINDING 8..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 87 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 117 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 119 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 123 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 123 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 124 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 127 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 175 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 260 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 272 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" SQ SEQUENCE 399 AA; 44026 MW; 0C8BC62464FB2C37 CRC64; MADRVVLAYS GGLDTSVAIS WIGKETGKEV VAVAIDLGQG GEDMEVVRQR ALDCGAVESV VVDARDEFAD EYCLPTIQAN ALYMDRYPLV SAISRPLIVK HLVEAARAHG GTTVAHGCTG KGNDQVRFEV GFGSLAPDLD VIAPVRDYAW TREKAIAFAE ENEIPINVSK KSPFSIDQNV WGRAVETGFL EDLWNAPTKD VYDYTQDPTV NWQAPDELII SFEAGRPVAI DGKPVSVLEA IQELNRRAGA QGVGRLDVVE DRLVGIKSRE IYEAPGAMVL INAHQELEHV TQERELGRYK RQTEQRWSEL VYDGLWFSPL KVALDTFIEK TQERVSGDIR LVLHGGAIIV NGRRSNESLY DFNLATYDEG DTFDQSYAKG FVQIHGLSSK VAAKRDLGL //