ID ASSY_THEMA Reviewed; 409 AA. AC Q9X2A1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 142. 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=TM_1780; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT. RG Joint center for structural genomics (JCSG); RT "Crystal structure of argininosuccinate synthase (TM1780) from Thermotoga RT maritima at 1.65 A resolution."; RL Submitted (MAR-2006) to the PDB data bank. 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 ECO:0000269|Ref.2}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. 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; AE000512; AAD36844.1; -; Genomic_DNA. DR PIR; H72210; H72210. DR RefSeq; NP_229577.1; NC_000853.1. DR RefSeq; WP_004082326.1; NZ_CP011107.1. DR PDB; 1VL2; X-ray; 1.65 A; A/B/C/D=1-409. DR PDBsum; 1VL2; -. DR AlphaFoldDB; Q9X2A1; -. DR SMR; Q9X2A1; -. DR STRING; 243274.TM_1780; -. DR PaxDb; 243274-THEMA_05300; -. DR EnsemblBacteria; AAD36844; AAD36844; TM_1780. DR KEGG; tma:TM1780; -. DR eggNOG; COG0137; Bacteria. DR InParanoid; Q9X2A1; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR EvolutionaryTrace; Q9X2A1; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Cytoplasm; Ligase; Nucleotide-binding; Reference proteome. FT CHAIN 1..409 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148656" FT BINDING 8..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 34 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 85 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 115 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 117 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 121 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 121 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 122 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 178 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 187 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 268 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 280 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 13..24 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 28..37 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 42..52 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 63..69 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:1VL2" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:1VL2" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 88..107 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 122..133 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 146..151 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 157..165 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 176..181 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:1VL2" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 229..235 FT /evidence="ECO:0007829|PDB:1VL2" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 245..258 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 263..269 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 271..281 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 283..299 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 302..321 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 327..340 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 345..352 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 355..362 FT /evidence="ECO:0007829|PDB:1VL2" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:1VL2" FT HELIX 383..404 FT /evidence="ECO:0007829|PDB:1VL2" SQ SEQUENCE 409 AA; 46054 MW; ECCDC8575E962482 CRC64; MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFVAIKEKAL KTGASKVYVE DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ VEIAEKEGAQ YVAHGATGKG NDQVRFELTY AALNPNLKVI SPWKDPEFLA KFKGRTDLIN YAMEKGIPIK VSKKRPYSED ENLMHISHEA GKLEDPAHIP DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT EKTDPLELFE YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS IYKGNVMPVA RYSPYSLYNP ELSSMDVEGG FDATDSKGFI NIHALRLKVH QLVKKGYQR //