ID ASSY_YERE8 Reviewed; 454 AA. AC A1JTL6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00581}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00581}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00581}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00581}; OrderedLocusNames=YE2680; OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / OS 8081). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=393305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 13174 / 8081; RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206; RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J., RA Prentice M.B.; RT "The complete genome sequence and comparative genome analysis of the high RT pathogenicity Yersinia enterocolitica strain 8081."; RL PLoS Genet. 2:2039-2051(2006). 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_00581}; 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_00581}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00581}. 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; AM286415; CAL12713.1; -; Genomic_DNA. DR RefSeq; WP_005165407.1; NC_008800.1. DR RefSeq; YP_001006871.1; NC_008800.1. DR AlphaFoldDB; A1JTL6; -. DR SMR; A1JTL6; -. DR KEGG; yen:YE2680; -. DR PATRIC; fig|393305.7.peg.2846; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_1_6; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000642; 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..454 FT /note="Argininosuccinate synthase" FT /id="PRO_1000025445" FT BINDING 17..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 99 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 131 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 135 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 135 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 136 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 139 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 192 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 201 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 203 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 280 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" SQ SEQUENCE 454 AA; 50708 MW; FE877449446A1EC7 CRC64; MTTILKHLPI NQRVGIAFSG GLDTSAALLW MQKKGAIPYA YTANLGQPDE EDYDAIPRKA MEYGAEKARL IDCRKQLVAE GIAAIQCGAF HNTTAGVTYF NTTPLGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLTNAE LKIYKPWLDT DFIDELGGRH EMSEFMIQSG FDYKMSTEKA YSTDSNMLGA THEAKDLEFL NSSVKIVNPI MGVKFWDENV VVKAEEVSVR FERGYPVALN GVVFDDSVEL MMEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL HIAYERLLTG IHNEDTIEQY HANGRVLGRL LYQGRWFDPQ ALMLRDSAQR WVASEITGEV TLELRRGNDY SILNTVSENL TYQPERLTME KGDSVFSPDD RIGQLTMRNL DITDTRKKLF SYATTGLLSA SAEVGLPQVD NNNLTARGLQ DKSK //