ID ASSY_DICT6 Reviewed; 397 AA. AC B5YAL9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 82. 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=DICTH_1677; OS Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12). OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae; OC Dictyoglomus. OX NCBI_TaxID=309799; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35947 / DSM 3960 / H-6-12; RX PubMed=24558247; DOI=10.1128/genomea.00109-14; RA Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N., RA Ward N., Robb F.T., Eisen J.A.; RT "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus RT thermophilum H-6-12."; RL Genome Announc. 2:0-0(2014). 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; CP001146; ACI19694.1; -; Genomic_DNA. DR RefSeq; WP_012548326.1; NC_011297.1. DR AlphaFoldDB; B5YAL9; -. DR SMR; B5YAL9; -. DR STRING; 309799.DICTH_1677; -. DR PaxDb; 309799-DICTH_1677; -. DR KEGG; dth:DICTH_1677; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_0; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000001733; 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding. FT CHAIN 1..397 FT /note="Argininosuccinate synthase" FT /id="PRO_1000191892" 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 257 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 269 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" SQ SEQUENCE 397 AA; 45126 MW; 520CF3723D55DBA0 CRC64; MKKEKVVLAY SGGLDTSVAI KWLMQKYSLD VITLTVDIGQ GINLDEIKNK AENLGVEKAY VLDLKEEFVK DYIIPAIKSN AMYERVYPLA TALSRPLIAK YLVKIAKENG AKYVAHGCTG KGNDQVRIDL GVKALAPDLE IIAPVREWNF SREEEIEYAL ENNIPIPVSR KSPYSIDENL WGRSIEGGIL EDPWQEPPED IYLWTRFENR EPSYIEITFE RGVPVELNGV RKDVVEIIEE LNKIAGSYGI GRIDHIENRL VGIKSREIYE APAAIVIIRA HEALEDMVLP RELAHYKKML EDKYAELVYY GLWFDPFREA LQAFMDKTQD RVTGKVKIKL LPWSFSIVGR ESPYSLYDHG LATYDKGSTF STESAVGFIK LFGLQNYLYA LKGGNND //