ID ASSY_XENLA Reviewed; 411 AA. AC Q7ZWM4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Argininosuccinate synthase {ECO:0000305}; DE EC=6.3.4.5 {ECO:0000250|UniProtKB:P00966}; DE AltName: Full=Citrulline--aspartate ligase; GN Name=ass1 {ECO:0000250|UniProtKB:P00966}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway CC transforming neurotoxic amonia produced by protein catabolism into CC inocuous urea in the liver of ureotelic animals. Catalyzes the CC formation of arginosuccinate from aspartate, citrulline and ATP and CC together with ASL it is responsible for the biosynthesis of arginine in CC most body tissues. {ECO:0000250|UniProtKB:P00966}. 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; CC Evidence={ECO:0000250|UniProtKB:P00966}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 2/3. CC {ECO:0000250|UniProtKB:P00966}. CC -!- PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L- CC arginino)succinate from L-aspartate and L-citrulline: step 1/1. CC {ECO:0000250|UniProtKB:P00966}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00966}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P00966}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. CC {ECO:0000305}. 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; BC046941; AAH46941.1; -; mRNA. DR RefSeq; NP_001080795.1; NM_001087326.1. DR AlphaFoldDB; Q7ZWM4; -. DR SMR; Q7ZWM4; -. DR DNASU; 380488; -. DR GeneID; 380488; -. DR KEGG; xla:380488; -. DR AGR; Xenbase:XB-GENE-17340606; -. DR CTD; 380488; -. DR Xenbase; XB-GENE-17340606; ass1.L. DR OrthoDB; 350199at2759; -. DR UniPathway; UPA00068; UER00113. DR UniPathway; UPA00158; UER00272. DR Proteomes; UP000186698; Chromosome 8L. DR Bgee; 380488; Expressed in camera-type eye and 15 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004055; F:argininosuccinate synthase activity; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006526; P:arginine biosynthetic process; ISS:UniProtKB. DR GO; GO:0000050; P:urea cycle; ISS:UniProtKB. 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 2: Evidence at transcript level; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome; Urea cycle. FT CHAIN 1..411 FT /note="Argininosuccinate synthase" FT /id="PRO_0000321324" FT BINDING 11..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 88 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 93 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 116..124 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 120 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 124 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 124 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 125 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 128 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 181 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 190 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 271 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" FT BINDING 283 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000250|UniProtKB:P00966" SQ SEQUENCE 411 AA; 46750 MW; 9A9F683A38A2378C CRC64; MSQSKGTVVL AYSGGLDTSC ILVWLKEQGF DVIAYLANIG QNEDFEEARK KAVNLGAKKV YIEDIRQQFV EEYIWPAVQA NAIYEDRYLL GTSLARPCIA KKQVEIAKKE AAEYVSHGAT GKGNDQIRFE LTCYSLYPEV KIIAPWRMPE FYNRFRGRSD LMEYAKKHNI SVPVTPKSPW SMDENLMHIS YEGGILENPK NHAPPGLYLK TKDPATSPDE PDILEIEFKK GVPVKVTNTK NKTQHSSSLA LFCYLNEVAG KHGVGRIDIV ENRFIGMKSR GIYETPAGTI LYQAHLDIEA FTMDREMRKI KQQLSQRFAE QIYNGFWYSP ECEFVRSCIS KSQEMVEGKV LVSVLKGQVY VLGREAPHSL YNEELVSMDV QGDYDPADAC GFIKINAVRL KEYHRLQKNK K //