ID ASSY_LEGPH Reviewed; 405 AA. AC Q5ZY78; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 110. 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=lpg0494; OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC OS 33152 / DSM 7513). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=272624; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513; RX PubMed=15448271; DOI=10.1126/science.1099776; RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A., RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., RA Russo J.J.; RT "The genomic sequence of the accidental pathogen Legionella pneumophila."; RL Science 305:1966-1968(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_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; AE017354; AAU26591.1; -; Genomic_DNA. DR RefSeq; WP_010946242.1; NC_002942.5. DR RefSeq; YP_094538.1; NC_002942.5. DR PDB; 6XNQ; X-ray; 1.95 A; A/B/C/D=1-405. DR PDB; 7K5Z; X-ray; 1.85 A; A/B/C/D=1-405. DR PDBsum; 6XNQ; -. DR PDBsum; 7K5Z; -. DR AlphaFoldDB; Q5ZY78; -. DR SMR; Q5ZY78; -. DR STRING; 272624.lpg0494; -. DR PaxDb; 272624-lpg0494; -. DR GeneID; 66489688; -. DR KEGG; lpn:lpg0494; -. DR PATRIC; fig|272624.6.peg.515; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_2_6; -. DR OrthoDB; 9801641at2; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000609; 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..405 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148604" FT BINDING 11..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 90 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 121 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 125 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 126 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 129 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 178 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 187 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 263 FT /ligand="L-citrulline" FT /ligand_id="ChEBI:CHEBI:57743" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00005" FT BINDING 275 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:7K5Z" FT HELIX 16..28 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 33..42 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 68..74 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 76..82 FT /evidence="ECO:0007829|PDB:7K5Z" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 96..110 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:6XNQ" FT HELIX 126..137 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 141..144 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 155..164 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 176..181 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 240..253 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 268..276 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 278..294 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 297..305 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 307..315 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 322..334 FT /evidence="ECO:0007829|PDB:7K5Z" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 340..347 FT /evidence="ECO:0007829|PDB:7K5Z" FT STRAND 350..357 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 379..388 FT /evidence="ECO:0007829|PDB:7K5Z" FT HELIX 390..398 FT /evidence="ECO:0007829|PDB:7K5Z" FT TURN 399..401 FT /evidence="ECO:0007829|PDB:7K5Z" SQ SEQUENCE 405 AA; 44985 MW; 6A76E7D62947DC56 CRC64; MKKVIKKIAL AYSGGLDTSI MIPWLKEHYE HAEVIAVICD LGQQEDLDAI KNKALKSGAS KAYVVDVKNE FATQYLWPLV KSGALYEDQY ILGTISRPLI AQKLVEIALT EQVNAVAHGA TGKGNDQVRF EYSIKALAPQ LEIIAPWRTW DIKSRQEAIV YAKAHGIEVP VTPKAPYSRD HNIWYISHEG GVLEDPSQEM PNDVLLMTAP VSQTPDEEEV VVLDFKKGVP VALNGQELSP VDLLNSLNQK AGQHGIGVAD IVENRLVGMK IRGIYEAPAA AVLYKAHKLL ESLCLTRSTL HLKQSLQQTY ANLVYEGRWF SQTKQALDAF IDVTQQHVTG CVKLKLFKGN IIPAGMHSPY SLHHPELATF EEDNVYNQKD AEGFINLFSL SAKIYSQVHQ GGNYD //