ID ASSY_BURPS Reviewed; 404 AA. AC Q63U95; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 100. 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=BPSL1721; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A., RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia RT pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). 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; BX571965; CAH35720.1; -; Genomic_DNA. DR RefSeq; WP_004521517.1; NZ_CP009538.1. DR RefSeq; YP_108321.1; NC_006350.1. DR AlphaFoldDB; Q63U95; -. DR SMR; Q63U95; -. DR STRING; 272560.BPSL1721; -. DR GeneID; 56529404; -. DR KEGG; bps:BPSL1721; -. DR PATRIC; fig|272560.51.peg.3814; -. DR eggNOG; COG0137; Bacteria. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000605; 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; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding; Reference proteome. FT CHAIN 1..404 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148579" FT BINDING 9..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 36 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 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" SQ SEQUENCE 404 AA; 44744 MW; DDDC9B73AC7EBA68 CRC64; MKPKHILLAY SGGLDTSTAL HFLKRHFDCR VTAYCANLGQ KEDWERMKRR AAIAGADELV IEDLRETFIG DFVFPALKAN ASYERDYLLG TPLARPAIVK GLIEYARKHD VDCLSHGCTQ KGNDQVRFEM AAKILAPDLP TVAPWRIWSL QSREDLFAYC QQHGIPVESR PDNLLSHDEN LVHITTEGDY LESVANAFDW RDANWITPPT QAPDAIETIT LGFRRGVPVS VDGAALGPVE LVERLNEAGA RNGVGFQDII ENRINGLKVR GVFENPALTI LHAAHRKLEK ITLGRDVERL RNLVSDDYGD IVYRGLWFSD ERLCLQALID ESQKYVSGDV KVQLYKGSCT PCAVESEQSL YSRELVTLHA GRAISGEDAT GFLNTLGLRI GIEAARAGNT GAGA //