ID ASSY_LEIXX Reviewed; 478 AA. AC Q6ACL1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 109. 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=Lxx21970; OS Leifsonia xyli subsp. xyli (strain CTCB07). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Leifsonia. OX NCBI_TaxID=281090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CTCB07; RX PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827; RA Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P., RA Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D., RA de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R., RA Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L., RA El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., RA Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., RA Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., RA Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., RA Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.; RT "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli RT subsp. xyli."; RL Mol. Plant Microbe Interact. 17:827-836(2004). 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_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; AE016822; AAT89882.1; -; Genomic_DNA. DR RefSeq; WP_011186866.1; NC_006087.1. DR AlphaFoldDB; Q6ACL1; -. DR SMR; Q6ACL1; -. DR STRING; 281090.Lxx21970; -. DR KEGG; lxx:Lxx21970; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_1_11; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000001306; 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:arginine biosynthetic process; IEA:UniProtKB-UniRule. 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; 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 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..478 FT /note="Argininosuccinate synthase" FT /id="PRO_1000025430" 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 478 AA; 52261 MW; 0EEDB08C898AE65C CRC64; MSKVLSSLPV GERVGIAFSG GLDTSCAVAW MREKGAVPCA YTADIGQYDE PNIEEVPGRA TEYGAEIARL VDAKRALVEE GLIALQCGAF HIRSGGKTYF NTTPLGRAVT GVMLVRAMRD DDVEIWGDGS TYKGNDIERF YRYGLIANPR LRIYKPWLDT AFVEELGGRT EISEWLVARG FPYRDATEKA YSTDANIWGA THEAKRLEEL DAGLDIVEPI MGVAAWREDI EVAPETVSVS FEYGRPVALN GIEFADPVAL VPEANAIGGR HGLGASDQIE NRIIEAKSRG IYEAPGMALL HIAYERLLNA IHNEDTVANY HTEGRRLGRL MYEGRWLDPQ SLMLRESLQR WVGSAITGEV TLRLRRGDDY TILDTTGPAL SYHPDKLSME RVGNAAFGPA DRIGQLTMRN LDIADSRSRL EQYAATGLIG GPTAELVGEL QEGSARSILE LDVSPEDDAL SREIDASSEG AAFDAGTD //