ID A0A068NEY8_9ACTO Unreviewed; 411 AA. AC A0A068NEY8; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 03-AUG-2022, entry version 34. 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 ORFNames=FB03_01650 {ECO:0000313|EMBL:AIE82188.1}; OS Actinotignum schaalii. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinotignum. OX NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82188.1, ECO:0000313|Proteomes:UP000035032}; RN [1] {ECO:0000313|EMBL:AIE82188.1, ECO:0000313|Proteomes:UP000035032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82188.1, RC ECO:0000313|Proteomes:UP000035032}; RX PubMed=25189588; RA Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M., RA Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M., RA Christensen J.J., Prag J., Thomsen T.R.; RT "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420."; RL Genome Announc. 2:e00880-14(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: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; CP008802; AIE82188.1; -; Genomic_DNA. DR RefSeq; WP_026428863.1; NZ_CP008802.1. DR EnsemblBacteria; AIE82188; AIE82188; FB03_01650. DR KEGG; asg:FB03_01650; -. DR OrthoDB; 357142at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000035032; 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; 3.40.50.620; -; 1. DR Gene3D; 3.90.1260.10; -; 1. DR HAMAP; MF_00005; Arg_succ_synth_type1; 1. 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 PANTHER; PTHR11587; PTHR11587; 1. DR Pfam; PF00764; Arginosuc_synth; 1. DR SUPFAM; SSF69864; SSF69864; 1. DR TIGRFAMs; TIGR00032; argG; 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}. FT BINDING 9..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 88 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 120 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" 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 124 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 128 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005" FT BINDING 176 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 411 AA; 45046 MW; 2F4BFF9524683C8E CRC64; MAKERVVLAY SGGLDTSVAI GWIGERTGAE VITVAVDVGQ GGEDLETIRQ RALDCGAVEA YIADARDEFA SEYCMPALKA GALYMDAYPL ISAISRPVIV KHLVAAARQF GATTVAHGCT GKGNDQVRFE NGITQLGPDL ACLSPVRDLA LTREFAIDYA NKHNLPIETT HHNPFSIDQN VWGRAIETGY LEDLWNAPTK DVYTYTDDPT YPPLPDEVII TFEGGIPVKI DGEAVTPLQA IEQLNKRAGK QGIGRIDVVE DRYVGIKSRE IYEAPGAMAL LTAHKELENV TMDREQARFK RTVTDRWADI VYEGQWFSPL KRSLDAYIED TQRYVSGDIR MVMHGGRATV TGRRSDASLY DFNLATYDAG DSFDQSHAKG FIELTGLPAK LAAARDVTFG RGVAIPPARL N //