ID ASSY_SERP5 Reviewed; 406 AA. AC A8GL82; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, 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=Spro_4779; OS Serratia proteamaculans (strain 568). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Yersiniaceae; Serratia. OX NCBI_TaxID=399741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568; RX PubMed=19060168; DOI=10.1128/aem.02239-08; RA Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N., RA Barac T., Vangronsveld J., van der Lelie D.; RT "Genome survey and characterization of endophytic bacteria exhibiting a RT beneficial effect on growth and development of poplar trees."; RL Appl. Environ. Microbiol. 75:748-757(2009). 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; CP000826; ABV43872.1; -; Genomic_DNA. DR AlphaFoldDB; A8GL82; -. DR SMR; A8GL82; -. DR STRING; 399741.Spro_4779; -. DR PaxDb; 399741-Spro_4779; -. DR KEGG; spe:Spro_4779; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_6; -. 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:000019; 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..406 FT /note="Argininosuccinate synthase" FT /id="PRO_1000057044" FT BINDING 12..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 92 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 97 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 122 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 128 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 129 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 132 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 181 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 190 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 266 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 278 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" SQ SEQUENCE 406 AA; 44973 MW; C1DBEC2A22CB2E39 CRC64; MQNQGIKKIV LAYSGGLDTS AIIPWLKENY GGCEVVAFVA DIGQERSDLE GVEQKALQSG ASECHVVDLR EEFIRDYVYP VLQTGALYEG SYLLGTSMAR PIIAKAQVEL ALKVGADAVC HGATGKGNDQ VRFETTYTAL APHLKVVAPW REWNLRSREA LLDYLKERNI PTTASLEKIY SRDENAWHIS TEGGVLESPW NAPNKDCWVW TVDPQEAPDQ PEQVTITVEK GCVVAVNGEA LSPYKCLETL NVLGAKHGVG RIDIVENRLV GIKSRGCYET PGGTIMVAAL RGVEQLVLDR DSFKWREQLG LEMSYVVYDG RWFAPLRRSL QASAEALAEE VNGEVVLQLY KGQVTAIQKK SANSLYSEEF ATFGEDEVYD HSHAGGFIRL FSLSSRIRAL NEIKNK //