ID ASSY_SULDN Reviewed; 404 AA. AC Q30QT1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 105. 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=Suden_1373; OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira OS denitrificans (strain ATCC 33889 / DSM 1251)). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Sulfurimonadaceae; Sulfurimonas. OX NCBI_TaxID=326298; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33889 / DSM 1251; RX PubMed=18065616; DOI=10.1128/aem.01844-07; RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J., RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A., RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E., RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A., RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D., RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.; RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas RT denitrificans."; RL Appl. Environ. Microbiol. 74:1145-1156(2008). 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; CP000153; ABB44650.1; -; Genomic_DNA. DR RefSeq; WP_011373002.1; NC_007575.1. DR AlphaFoldDB; Q30QT1; -. DR SMR; Q30QT1; -. DR STRING; 326298.Suden_1373; -. DR KEGG; tdn:Suden_1373; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_7; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000002714; 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 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm; KW Ligase; Nucleotide-binding; Reference proteome. FT CHAIN 1..404 FT /note="Argininosuccinate synthase" FT /id="PRO_0000263991" 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" SQ SEQUENCE 404 AA; 45383 MW; 32B80912FE65255C CRC64; MKREVKKVVL AYSGGLDTSV ILKWLQDEYK CEVVTFTADI GQGEEVEPAR AKALALGIKP ENIFIDDLRE EFVKDYVFPM FRANAIYEGE YLLGTSIARP LIAKRQVEIA HLTNADGVSH GATGKGNDQV RFEMGYLSKD STLTVIAPWR EWDLNSREKL LAYAEEHGIQ IEKKGKKSPY SMDANLLHIS YEGGILEDPN AEPEDSMWLW TTKPEDAPNT PEYITIGYEN GDPVSLNGEK LTPATMLETL NKIAGKHGIG RADIVENRYV GMKSRGCYET PGGTIMLKGH RAIESITLDR EEAHLKDELM PRYAKLIYNG FWFSPEREML QAAIDTTQKN VKGSVKLKLY KGSVMVVGRS SEFSLFNPEY CTFEEDAVYD QKDAAGFIKL NALRFIIAGK ARKK //