ID ASSY_METMP Reviewed; 397 AA. AC P61527; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 27-MAR-2024, entry version 106. 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=MMP0073; OS Methanococcus maripaludis (strain S2 / LL). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=267377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2 / LL; RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004; RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., RA Olson M.V., Leigh J.A.; RT "Complete genome sequence of the genetically tractable hydrogenotrophic RT methanogen Methanococcus maripaludis."; RL J. Bacteriol. 186:6956-6969(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; BX950229; CAF29629.1; -; Genomic_DNA. DR RefSeq; WP_011170017.1; NC_005791.1. DR AlphaFoldDB; P61527; -. DR SMR; P61527; -. DR STRING; 267377.MMP0073; -. DR EnsemblBacteria; CAF29629; CAF29629; MMP0073. DR GeneID; 2761944; -. DR KEGG; mmp:MMP0073; -. DR PATRIC; fig|267377.15.peg.74; -. DR eggNOG; arCOG00112; Archaea. DR HOGENOM; CLU_032784_4_2_2; -. DR OrthoDB; 5877at2157; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000590; 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: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..397 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148679" FT BINDING 9..17 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 175 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 184 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 260 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 272 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" SQ SEQUENCE 397 AA; 44580 MW; E91F6F998F72F667 CRC64; MQEKIAVLAY SGGLDTSCCL KLLEDKYDYK VISVAVDVGQ PEDDLKEPEE KAKKFGVLKH YTIDAKEEFA KDYIFRAIKA NALYEGYPLS TALARPLIAI KIAELAQEVG ASAISHGCTG KGNDQFRFES VMRAKTPEIE IVAPIRDLNL TRTEEIAYAK EKGIPVPVDL EKPFSIDENL WGRSIEGGIL EDPMTETPKE CFAWTVDPTD AQDKEEYVEI DFEEGVPVAI NGDALEAVSL IRKVNEIAGR NGVGRVDIVE DRVLGLKSRE NYECPGAMLL ITAHKALEQL VLTREELVFK EMVDSKYADL VYKGLWHEPL RLDLDAFIDK TQTRMNGKVV LKLYKGSMRI AGRESKDAIY NEEMVSFENK EMDQREIVGM VKFHGLQAAI YEGLTRK //