ID ASSY_DICCH Reviewed; 242 AA. AC P0C1A0; P42181; Q9KHB9; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 24-JAN-2024, entry version 50. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; DE Flags: Fragment; GN Name=argG; OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Dickeya. OX NCBI_TaxID=556; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=RA3B; RA Huang H.-C., Chu M.-K., Hsu S.-T., Tzeng K.-C., Lin R.-H.; RT "Molecular cloning of genes involved in blue pigment synthesis from Erwinia RT chrysanthemi RA3B."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. 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; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 2/3. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2 CC subfamily. {ECO:0000305}. 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; AF265211; AAF74776.1; -; Genomic_DNA. DR AlphaFoldDB; P0C1A0; -. DR SMR; P0C1A0; -. DR UniPathway; UPA00068; UER00113. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.287.400; -; 1. DR Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1. DR InterPro; IPR048268; Arginosuc_syn_C. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR024073; AS_multimer_C_tail. DR PANTHER; PTHR11587; ARGININOSUCCINATE SYNTHASE; 1. DR PANTHER; PTHR11587:SF2; ARGININOSUCCINATE SYNTHASE; 1. DR Pfam; PF20979; Arginosuc_syn_C; 1. DR SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding. FT CHAIN <1..242 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148699" FT NON_TER 1 SQ SEQUENCE 242 AA; 27349 MW; BF3C91A7FD7D49D5 CRC64; EFLNSSVKIV NPIMGVKFWD ENVRIPAEEV TVRFERGHPV ALNGQTFSDD VELLLEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM ALLHIAYERL VTGIHNEDTI EQYHAHGRQL GRLLYQGRWF DPQALMLRDA LQRWVASEIT GEVTLELRRG NDYSILNTVS DNLTYKPERL TMEKGESVFS PDDRIGQLTM RNLDITDTRE KLFNYVESGL ISSGNAGLPQ VANPLLQDKS AK //