ID ASSY_BURML STANDARD; PRT; 445 AA. AC P59608; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate DE ligase). GN Name=argG; OS Burkholderia multivorans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=87883; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17616; RX MEDLINE=22638290; PubMed=12754231; RX DOI=10.1128/JB.185.11.3333-3343.2003; RA Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.; RT "Distribution and organization of auxotrophic genes on the RT multichromosomal genome of Burkholderia multivorans ATCC 17616."; RL J. Bacteriol. 185:3333-3343(2003). CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + (N(omega)-L-arginino)succinate. CC -!- PATHWAY: Arginine biosynthesis; seventh step. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable). CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 2 subfamily. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; AB091438; BAC65286.1; -. DR HSSP; P22767; 1KP3. DR HAMAP; MF_00581; -; 1. DR InterPro; IPR001518; Arginosuc_synth. DR Pfam; PF00764; Arginosuc_synth; 1. DR TIGRFAMs; TIGR00032; argG; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. KW Arginine biosynthesis; ATP-binding; Ligase. FT SITE 99 99 Citrulline binding (By similarity). FT SITE 131 131 Aspartate binding (By similarity). FT SITE 135 135 Citrulline and aspartate binding (By FT similarity). FT SITE 136 136 Aspartate binding (By similarity). FT SITE 139 139 Citrulline binding (By similarity). FT SITE 192 192 Citrulline binding (By similarity). FT SITE 201 201 Citrulline binding (By similarity). FT SITE 203 203 Citrulline binding (By similarity). FT SITE 280 280 Citrulline binding (By similarity). FT BINDING 17 17 ATP (By similarity). FT BINDING 43 43 ATP (By similarity). FT BINDING 129 129 ATP (By similarity). FT BINDING 131 131 ATP (By similarity). FT BINDING 136 136 ATP (By similarity). FT BINDING 194 194 ATP (By similarity). SQ SEQUENCE 445 AA; 49252 MW; 67581060BC11267F CRC64; MSTILESLPT GQKVGIAFSG GLDTSAALHW MKLKGAVPYA YTANLGQPDE DDYDAIPKRA LEYGAAGARL IDCRAQLVAE GIAALQSGAF HITTAGVTYF NTTPIGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLVNPD LKIYKPWLDQ TFIDELGGRA EMSEFMRQSG FAYKMSAEKA YSTDSNLLGA THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIAAEEVTVR FEAGQPVALN GVEFKDQVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR WVARAITGEV KIELRRGNDY SILSTKSPNL TYQPERLSME KVASTFSPRD RIGQLTMRNL DITDTRDKLR VYTQVGLLTP GEASALPQIK GDSGE //