ID ASSY_BORPE Reviewed; 445 AA. AC Q7VTJ9; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 117. 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}; OrderedLocusNames=BP3537; OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257313; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). 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; BX640421; CAE43796.1; -; Genomic_DNA. DR RefSeq; NP_882052.1; NC_002929.2. DR RefSeq; WP_003820367.1; NZ_CP039022.1. DR PDB; 5US8; X-ray; 2.15 A; A/B=1-445. DR PDB; 6E5Y; X-ray; 1.50 A; A=1-445. DR PDBsum; 5US8; -. DR PDBsum; 6E5Y; -. DR AlphaFoldDB; Q7VTJ9; -. DR SMR; Q7VTJ9; -. DR STRING; 257313.BP3537; -. DR PaxDb; 257313-BP3537; -. DR GeneID; 69600464; -. DR KEGG; bpe:BP3537; -. DR PATRIC; fig|257313.5.peg.3829; -. DR eggNOG; COG0137; Bacteria. DR HOGENOM; CLU_032784_4_1_4; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000002676; 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 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..445 FT /note="Argininosuccinate synthase" FT /id="PRO_0000148692" 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" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 22..33 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 37..44 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 55..63 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 74..86 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:5US8" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:5US8" FT HELIX 102..120 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 136..147 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 160..165 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 169..178 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 235..242 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 257..269 FT /evidence="ECO:0007829|PDB:6E5Y" FT TURN 270..274 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 295..311 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 314..332 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 339..351 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 358..364 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 370..376 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:6E5Y" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 399..407 FT /evidence="ECO:0007829|PDB:6E5Y" FT HELIX 410..425 FT /evidence="ECO:0007829|PDB:6E5Y" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:6E5Y" SQ SEQUENCE 445 AA; 49323 MW; 81278F1EBC07CE61 CRC64; MTTILPNLPT GQKVGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE PDYDEIPRRA MQYGAEAARL VDCRAQLVAE GIAALQAGAF HISTAGLTYF NTTPIGRAVT GTMLVAAMKE DGVNIWGDGS TFKGNDIERF YRYGLLTNPD LKIYKPWLDQ TFIDELGGRA EMSEYMRQAG FDYKMSAEKA YSTDSNMLGA THEAKDLELL SAGIRIVQPI MGVAFWQDSV QIKAEEVTVR FEEGQPVALN GVEYADPVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL FIAYERLVTG IHNEDTIEQY RENGRKLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV TLELRRGNDY SLLNTESANL TYAPERLSME KVENAPFTPA DRIGQLTMRN LDIVDTREKL FTYVKTGLLA PSAGSALPQI KDGKK //