ID C7N012_SACVD Unreviewed; 402 AA. AC C7N012; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Argininosuccinate synthase {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916, ECO:0000256|HAMAP-Rule:MF_00005}; GN Name=argG {ECO:0000256|HAMAP-Rule:MF_00005}; GN OrderedLocusNames=Svir_25570 {ECO:0000313|EMBL:ACU97548.1}; OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC OS 12207 / P101). OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharomonospora. OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU97548.1, ECO:0000313|Proteomes:UP000000841}; RN [1] {ECO:0000313|EMBL:ACU97548.1, ECO:0000313|Proteomes:UP000000841} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101 RC {ECO:0000313|Proteomes:UP000000841}; RX PubMed=21304650; DOI=10.4056/sigs.20263; RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A., RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D., RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N., RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Saccharomonospora viridis type strain RT (P101)."; RL Stand. Genomic Sci. 1:141-149(2009). 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:0000256|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. CC {ECO:0000256|ARBA:ARBA00004967, ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00005}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP001683; ACU97548.1; -; Genomic_DNA. DR RefSeq; WP_015786860.1; NC_013159.1. DR AlphaFoldDB; C7N012; -. DR STRING; 471857.Svir_25570; -. DR KEGG; svi:Svir_25570; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_11; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000841; 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00005}; KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP- KW Rule:MF_00005}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00005}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00005}; Reference proteome {ECO:0000313|Proteomes:UP000000841}. FT DOMAIN 4..165 FT /note="Arginosuccinate synthase-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00764" FT DOMAIN 174..391 FT /note="Arginosuccinate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF20979" FT BINDING 8..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 87 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 117 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 119 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 123 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 123 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 124 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 127 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 175 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 260 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 272 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" SQ SEQUENCE 402 AA; 44302 MW; C9CE00DFED953A3E CRC64; MTERVVLAYS GGLDTSVAIG WIAEETGAEV VAVAVDVGQG GEDMETIRKR ALECGAVEAV VSDAKDEFAE EYCLPALQAN ALYMDRYPLV SALSRPLIVK HLVRAAERYG ATTVAHGCTG KGNDQVRFEV GIGALAPDLK VIAPVRDFAW TREKAISWAE ERNLPIDVTK KSPFSIDQNV WGRAVETGVL EDLWNEPPKE VYSYTQDPTV HFQAPDEVII TFEKGVPVAI DGKKVTVLEA IQEMNQRAGA HGIGRLDMVE DRLVGIKSRE VYEAPGAIAL ITAHQELENV TVERDLARFK RQVEQRWGEL VYDGLWFSPL KDALDGFIAK AQEHVSGDIR MVLHGGTATV TGRRSDESLY DFNLATYDEG DTFDQSLAKG FVQLWGLPSK IAAKRQQNKN NN //