ID ASSY_CAMJE Reviewed; 406 AA. AC Q9PHK7; Q0PAK8; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00005}; GN OrderedLocusNames=Cj0665c; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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_00005}; 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_00005}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 CC subfamily. {ECO:0000255|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; AL111168; CAL34806.1; -; Genomic_DNA. DR PIR; C81415; C81415. DR RefSeq; WP_002852200.1; NZ_SZUC01000002.1. DR RefSeq; YP_002344089.1; NC_002163.1. DR PDB; 4NZP; X-ray; 2.31 A; A=1-406. DR PDBsum; 4NZP; -. DR AlphaFoldDB; Q9PHK7; -. DR SMR; Q9PHK7; -. DR IntAct; Q9PHK7; 42. DR STRING; 192222.Cj0665c; -. DR PaxDb; 192222-Cj0665c; -. DR EnsemblBacteria; CAL34806; CAL34806; Cj0665c. DR GeneID; 904988; -. DR KEGG; cje:Cj0665c; -. DR PATRIC; fig|192222.6.peg.657; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_7; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000799; 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Cytoplasm; Ligase; Nucleotide-binding; Reference proteome. FT CHAIN 1..406 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148580" FT BINDING 11..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 38 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 91 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 96 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 123 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 127 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 127 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 128 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 131 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 181 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 190 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 266 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 278 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 16..28 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 32..41 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 47..55 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 69..75 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 77..81 FT /evidence="ECO:0007829|PDB:4NZP" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:4NZP" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 94..113 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 128..139 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 148..151 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 158..166 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 194..197 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:4NZP" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 222..229 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 243..256 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 261..267 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 269..279 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 281..297 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 300..319 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 325..336 FT /evidence="ECO:0007829|PDB:4NZP" FT TURN 337..340 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 343..350 FT /evidence="ECO:0007829|PDB:4NZP" FT STRAND 353..360 FT /evidence="ECO:0007829|PDB:4NZP" FT HELIX 382..401 FT /evidence="ECO:0007829|PDB:4NZP" SQ SEQUENCE 406 AA; 45578 MW; 8A1E137AF30EC77F CRC64; MKNEVKKVVL AYSGGLDTSI ILKWLQDEYN CEVVTFTADI GQGEELEPAR KKALSLGIKE ENIFIKDLRD EFVKDYVFPM FRANAIYEGE YLLGTSIARP LIAKTQAQIA LQTGADAVSH GATGKGNDQV RFELGYLAFS PDLKIIAPWR EWDLNSREKL LAYAQKHGID ISKKKGKSPY SMDANLLHIS YEGLVLEDPA HAPEEDMWRW SKSPKDAPNE SEIIELDFQK GDLVAINGEK LSPAGLLTKL NELGCKHGIG RLDIVENRYV GMKSRGCYET PGGTILLKAH RALESITLDR EAAHLKDELM PKYASLIYNG YWFSPERMML QALIDESQIH ANGRVKLELY KGNVMVIGRE SANDSLFNAA YCTFEEDEVY NQKDAAGFIK LNALRFIIAG KNGRKF //