ID ASSY_SACEN Reviewed; 472 AA. AC A4FDS0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 99. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00581}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00581}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00581}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00581}; GN OrderedLocusNames=SACE_2917; OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / OS NBRC 13426 / NCIMB 8594 / NRRL 2338). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Saccharopolyspora. OX NCBI_TaxID=405948; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / RC NRRL 2338; RX PubMed=17369815; DOI=10.1038/nbt1297; RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., RA Haydock S.F., Leadlay P.F.; RT "Complete genome sequence of the erythromycin-producing bacterium RT Saccharopolyspora erythraea NRRL23338."; RL Nat. Biotechnol. 25:447-453(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-citrulline + L-aspartate + ATP = 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_00581}; 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_00581}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00581}. 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; AM420293; CAM02195.1; -; Genomic_DNA. DR RefSeq; WP_009949409.1; NC_009142.1. DR AlphaFoldDB; A4FDS0; -. DR SMR; A4FDS0; -. DR STRING; 405948.SACE_2917; -. DR GeneID; 306459640; -. DR KEGG; sen:SACE_2917; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_1_11; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000006728; 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:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0000050; P:urea cycle; IEA:TreeGrafter. DR CDD; cd01999; ASS; 1. DR Gene3D; 1.10.287.400; -; 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_00581; Arg_succ_synth_type2; 1. DR InterPro; IPR023437; Arg_succ_synth_type2_subfam. 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; IPR024073; AS_multimer_C_tail. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00032; argG; 1. DR NCBIfam; NF003779; PRK05370.1; 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; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding; Reference proteome. FT CHAIN 1..472 FT /note="Argininosuccinate synthase" FT /id="PRO_1000025440" FT REGION 453..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 17..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 99 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 131 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 135 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 135 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 136 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 139 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 192 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 201 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 203 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" FT BINDING 280 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00581" SQ SEQUENCE 472 AA; 51621 MW; A3B786081009BCDA CRC64; MSKVLTSLPV GQRVGIAFSG GLDTSVAVAW MRENGAVPCT YTADIGQYDE SDIASIPGRA EAYGAEISRL VDCREALVEE GLAALSCGAF HIRSGGRTYF NTTPLGRAVT ATLLVRAMLA DDVLIWGDGS TFKGNDIERF YRYGLLANPR LRIYKPWLDT AFVGELGGRK EMSEWLQERD LPYRDSAEKA YSTDANIWGA THEAKKLEHL DTGIEIVDPI MGVPFWDDSV EIATEDVTLS FVQGRPVAIN GKEFDSPVDL VHEANAVGGR HGLGMSDQIE NRIIEAKSRG IYEAPGMALL FIAYERLVNA IHNEDTIASY HNEGRRLGRL MYEGRWFDPQ SLMLRESLQR WVGSAVTGEV TLRLRRGEDY SILDTTGPAF SYHPDKLSME RTEDAAFGPV DRIGQLTMRN LDIADSRAKL ENYAQLGLVG QAQAELVGSL QSGGAEAIAS VGTHEESDAG ALDRAAMESG TD //