ID ASSY_CLOBH Reviewed; 397 AA. AC A5I5A4; A7G6G7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 92. 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=CBO2670, CLC_2544; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A., RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain RT Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). 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: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; CP000727; ABS37966.1; -; Genomic_DNA. DR EMBL; AM412317; CAL84231.1; -; Genomic_DNA. DR RefSeq; WP_011986966.1; NC_009698.1. DR RefSeq; YP_001255169.1; NC_009495.1. DR RefSeq; YP_001388382.1; NC_009698.1. DR AlphaFoldDB; A5I5A4; -. DR SMR; A5I5A4; -. DR GeneID; 5186925; -. DR KEGG; cbh:CLC_2544; -. DR KEGG; cbo:CBO2670; -. DR PATRIC; fig|413999.7.peg.2653; -. DR HOGENOM; CLU_032784_4_2_9; -. DR UniPathway; UPA00068; UER00113. DR PRO; PR:A5I5A4; -. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. 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 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 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..397 FT /note="Argininosuccinate synthase" FT /id="PRO_0000321307" FT BINDING 8..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 86 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 91 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 118 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 122 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 122 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" 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 126 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 184 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 397 AA; 44731 MW; 762341059F7DF962 CRC64; MKEKVVLAYS GGLDTSIIIP WLKENYDLDV IAVCVNVGQG DDMDYVKTKA IKSGASKIYV EDVKEEFVVD YLYKAIKSEA LYEQDYMLGT SFARPLMAKK LVEIAHKEQA KYICHGCTGK GNDQVRFEVG VKAQDPTIKI IAPWRIWDIK SREDAIDYAK KVGVEVPVTK KKIYSVDKNL WHVSHEGGDL EDLKNEHKED MYFMVTPPEK AKDEPTYLEI YFEKGAPVKI NGEVLNPVDI IDKLNTIGGE NGIGIADIIE NRLVGMKSRG IYETPAGTLL YAAHKKLESV TLDKYTYQYK KIVSAQYGEL VYNGLWFTSL REAIDAFVDK TQENVTGTVQ LKLYKGNIKP CSVDTEYALY DEGISSFGES ELYSHKDAEG FINLFGLPSK IKALKNF //