ID ASSY_THET8 Reviewed; 400 AA. AC P59846; Q5SLK9; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2003, sequence version 1. DT 27-MAR-2024, entry version 129. 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=TTHA0284; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATE RP ANALOGS, AND SUBUNIT. RX PubMed=11844799; DOI=10.1074/jbc.m112430200; RA Goto M., Nakajima Y., Hirotsu K.; RT "Crystal structure of argininosuccinate synthetase from Thermus RT thermophilus HB8. Structural basis for the catalytic action."; RL J. Biol. Chem. 277:15890-15896(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP AND SUBSTRATES, RP AND SUBUNIT. RX PubMed=12684518; DOI=10.1074/jbc.m213198200; RA Goto M., Omi R., Miyahara I., Sugahara M., Hirotsu K.; RT "Structures of argininosuccinate synthetase in enzyme-ATP substrates and RT enzyme-AMP product forms: stereochemistry of the catalytic reaction."; RL J. Biol. Chem. 278:22964-22971(2003). 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|PubMed:11844799, ECO:0000269|PubMed:12684518}. 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; AP008226; BAD70107.1; -; Genomic_DNA. DR RefSeq; WP_011227831.1; NC_006461.1. DR RefSeq; YP_143550.1; NC_006461.1. DR PDB; 1J1Z; X-ray; 2.10 A; A/B/C/D=1-400. DR PDB; 1J20; X-ray; 2.00 A; A/B/C/D=1-400. DR PDB; 1J21; X-ray; 2.20 A; A/B/C/D=1-400. DR PDB; 1KH1; X-ray; 2.30 A; A/B/C/D=1-400. DR PDB; 1KH2; X-ray; 2.30 A; A/B/C/D=1-400. DR PDB; 1KH3; X-ray; 2.15 A; A/B/C/D=1-400. DR PDB; 1KOR; X-ray; 1.95 A; A/B/C/D=1-400. DR PDBsum; 1J1Z; -. DR PDBsum; 1J20; -. DR PDBsum; 1J21; -. DR PDBsum; 1KH1; -. DR PDBsum; 1KH2; -. DR PDBsum; 1KH3; -. DR PDBsum; 1KOR; -. DR AlphaFoldDB; P59846; -. DR SMR; P59846; -. DR DrugBank; DB02267; Argininosuccinate. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR EnsemblBacteria; BAD70107; BAD70107; BAD70107. DR GeneID; 3168176; -. DR KEGG; ttj:TTHA0284; -. DR PATRIC; fig|300852.9.peg.284; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_0; -. DR PhylomeDB; P59846; -. DR BRENDA; 6.3.4.5; 2305. DR UniPathway; UPA00068; UER00113. DR EvolutionaryTrace; P59846; -. DR Proteomes; UP000000532; 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 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..400 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148658" FT BINDING 6..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005, FT ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005, FT ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518" FT BINDING 84 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 89 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005, FT ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518" FT BINDING 116 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT BINDING 120 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT BINDING 120 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 121 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT BINDING 124 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 173 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 182 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 258 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT BINDING 270 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 27..36 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 41..51 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 62..68 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 70..75 FT /evidence="ECO:0007829|PDB:1KOR" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:1KOR" FT TURN 87..90 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 91..106 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 109..112 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:1J21" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 150..159 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 186..189 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 214..221 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 224..228 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 235..248 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 265..271 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 273..289 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 292..311 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 317..330 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 335..342 FT /evidence="ECO:0007829|PDB:1KOR" FT STRAND 345..352 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:1KOR" FT HELIX 373..394 FT /evidence="ECO:0007829|PDB:1KOR" SQ SEQUENCE 400 AA; 44816 MW; A4DAC90A7C5185C6 CRC64; MKIVLAYSGG LDTSIILKWL KETYRAEVIA FTADIGQGEE VEEAREKALR TGASKAIALD LKEEFVRDFV FPMMRAGAVY EGYYLLGTSI ARPLIAKHLV RIAEEEGAEA IAHGATGKGN DQVRFELTAY ALKPDIKVIA PWREWSFQGR KEMIAYAEAH GIPVPVTQEK PYSMDANLLH ISYEGGVLED PWAEPPKGMF RMTQDPEEAP DAPEYVEVEF FEGDPVAVNG ERLSPAALLQ RLNEIGGRHG VGRVDIVENR FVGMKSRGVY ETPGGTILYH ARRAVESLTL DREVLHQRDM LSPKYAELVY YGFWYAPERE ALQAYFDHVA RSVTGVARLK LYKGNVYVVG RKAPKSLYRQ DLVSFDEAGG YDQKDAEGFI KIQALRLRVR ALVEREGHGA //