ID ASSY_AGRFC Reviewed; 407 AA. AC Q8UC31; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 2. DT 27-MAR-2024, entry version 123. 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=Atu2667; ORFNames=AGR_C_4836; OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens OS (strain C58)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium; OC Agrobacterium tumefaciens complex. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., RA Gordon M.P., Olson M.V., Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C58 / ATCC 33970; RX PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). 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; AE007869; AAK88389.2; -; Genomic_DNA. DR PIR; AB2904; AB2904. DR PIR; D97679; D97679. DR RefSeq; NP_355604.2; NC_003062.2. DR RefSeq; WP_010972477.1; NC_003062.2. DR AlphaFoldDB; Q8UC31; -. DR SMR; Q8UC31; -. DR STRING; 176299.Atu2667; -. DR EnsemblBacteria; AAK88389; AAK88389; Atu2667. DR GeneID; 66222852; -. DR KEGG; atu:Atu2667; -. DR PATRIC; fig|176299.10.peg.2675; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_5; -. DR OrthoDB; 9801641at2; -. DR PhylomeDB; Q8UC31; -. DR BioCyc; AGRO:ATU2667-MONOMER; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000813; Chromosome circular. 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 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..407 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148560" FT BINDING 13..21 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 91 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 96 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 127 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 128 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 131 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 182 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 191 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 267 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 279 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" SQ SEQUENCE 407 AA; 45131 MW; 4B850FCBACE539B1 CRC64; MALPKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP ARKKAEMLGI KEIFVEDVRE EFVRDFVFPM FRANAVYEGV YLLGTSIARP LISKHLIEIA KKTGADAIAH GATGKGNDQV RFELSAYALN PDIKIIAPWR DWTFKSRTDL LNFAEQHQIP VAKDKKGEAP FSVDANLLHS SSEGKVLEDP AVEAPEYVHM RTISPEAAPD KATVIKVGFR KGDACSINGV EMSPATLLAT LNNYGRENGI GRLDLVENRF VGMKSRGVYE TPGGTILLAA HRAIESITLD RGAAHLKDDL MPRYAELIYY GFWFSPEREM LQALIDKSQE HVEGEVTLKL YKGNVMVTGR ESEKSLYSDA LVTFEDDHGA YDQKDAAGFI KLNALRLRTL AKRNLNK //