ID ASSY_RALN1 Reviewed; 445 AA. AC Q8XWC1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=argG; OrderedLocusNames=RSc2553; ORFNames=RS00732; OS Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000; RX PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M., RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M., RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M., RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P., RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). 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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 2/3. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 CC subfamily. {ECO:0000305}. 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; AL646052; CAD16260.1; -; Genomic_DNA. DR RefSeq; WP_011002468.1; NC_003295.1. DR AlphaFoldDB; Q8XWC1; -. DR SMR; Q8XWC1; -. DR STRING; 267608.RSc2553; -. DR EnsemblBacteria; CAD16260; CAD16260; RSc2553. DR GeneID; 60502059; -. DR KEGG; rso:RSc2553; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_1_4; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000001436; 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:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.287.400; -; 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_00581; Arg_succ_synth_type2; 1. DR InterPro; IPR023437; Arg_succ_synth_type2_subfam. 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; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR024073; AS_multimer_C_tail. 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; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding. FT CHAIN 1..445 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148704" FT BINDING 17..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 99 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" FT BINDING 136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 136 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 201 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" FT BINDING 203 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250" SQ SEQUENCE 445 AA; 49300 MW; 1F73F180ED2543B7 CRC64; METILQHVPV GQKVGIAFSG GLDTSAALRW MKNKGALPYA YTANLGQPDE EDYDAIPRKA LEYGAEKARL IDCRPQLANE GIAAIQAGAF HISTGGITYF NTTPLGRAVT GTMLVAAMKE DDVHIWGDGS TFKGNDIERF YRYGLLTNPA LKIYKPWLDQ TFIDELGGRA EMSAFMTKEG FGYKMSAEKA YSTDSNMLGA THEAKDLEHL NSGIRIVNPI MGVAFWKPEV EVKAEEVSIT FDEGRPVAVN GREIADPVEM FLELNRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL HIAYERLVTG IHNEDTIEQY RINGLRLGRL LYQGRWFDPQ AIMLRETAQR WVARAVTGTV TLELRRGNDY SILNTESPNL TYAPERLSME KVEDAPFSPA DRIGQLTMRN LDLMDTRDKL AIYSKAGLLS LGTSSALPQL GGDKK //