ID ASSY_LACPL Reviewed; 411 AA. AC P59603; F9ULZ9; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 1. DT 02-SEP-2026, entry version 121. 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=lp_0775; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=22156394; DOI=10.1128/jb.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). 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; AL935263; CCC78238.1; -; Genomic_DNA. DR RefSeq; WP_003641033.1; NC_004567.2. DR AlphaFoldDB; P59603; -. DR SMR; P59603; -. DR STRING; 220668.lp_0775; -. DR EnsemblBacteria; CCC78238; CCC78238; lp_0775. DR GeneID; 77217299; -. DR KEGG; lpl:lp_0775; -. DR PATRIC; fig|220668.9.peg.655; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_9; -. DR OrthoDB; 9801641at2; -. DR PhylomeDB; P59603; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000432; 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:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0000050; P:urea cycle; IEA:TreeGrafter. DR CDD; cd01999; ASS; 1. DR FunFam; 1.20.5.470:FF:000002; Argininosuccinate synthase; 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; Reference proteome. FT CHAIN 1..411 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148602" FT BINDING 11..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 88 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 120 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" 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 124 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 128 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 176 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 261 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 273 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" SQ SEQUENCE 411 AA; 45154 MW; 4198183D3BFF93E5 CRC64; MVKQNDKIIL AYSGGLDTSV AISWLKDKGY DVVACGIDVG EGKDMDAIKE KALKLGAVSS YMIDAKQEFA EEYALIALQG HTLYEGEYPL VSALSRPLIA KKLVTLAKQE HAVAIAHGCT GKGNDQVRFE VAIHALAPDI KIEAPVRDWH WSREEEIDYA KEHNIPVPIN LDSPYSIDEN LWGRANECGI LEDPWQGAPA DAFDRTKALA DTPDTPTTLE ITFEAGVPVA LDGESLNLAD LIIKLDQIAG EHGIGRIDHI ENRLVGIKSR EVYEAPAATV LLKAHKDLED LTFERELAHF KPIIEQKLAD TIYNGLWFSP LMEAMVAFLK QTQQVVNGVV RVQLFKGNVI TEGRKSPNSL YDTNLATYTS ADSFDQQAAV GFIKLWGLPT QVNAQVQAKA QAEAKTDKAH A //