ID ASSY_BURTA Reviewed; 446 AA. AC Q2T1W2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=argG; OrderedLocusNames=BTH_I0279; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., RA Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., RA Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., RA Roberts K., Hatch B., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 2 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000086; ABC37394.1; -; Genomic_DNA. DR RefSeq; YP_440837.1; -. DR SMR; Q2T1W2; 2-444. DR GeneID; 3848636; -. DR GenomeReviews; CP000086_GR; BTH_I0279. DR KEGG; bte:BTH_I0279; -. DR TIGR; BTH_I0279; -. DR HOGENOM; Q2T1W2; -. DR OMA; Q2T1W2; GGRKEMS. DR BioCyc; BTHA271848:BTH_I0279-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00581; -; 1. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR PANTHER; PTHR11587; Arginosuc_synth; 1. DR Pfam; PF00764; Arginosuc_synth; 2. DR TIGRFAMs; TIGR00032; argG; 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; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding. FT CHAIN 1 446 Argininosuccinate synthase. FT /FTId=PRO_1000025418. FT NP_BIND 17 25 ATP (By similarity). FT BINDING 43 43 ATP (By similarity). FT BINDING 99 99 Citrulline (By similarity). FT BINDING 129 129 ATP; via amide nitrogen (By similarity). FT BINDING 131 131 Aspartate (By similarity). FT BINDING 131 131 ATP (By similarity). FT BINDING 135 135 Aspartate (By similarity). FT BINDING 135 135 Citrulline (By similarity). FT BINDING 136 136 Aspartate (By similarity). FT BINDING 136 136 ATP (By similarity). FT BINDING 139 139 Citrulline (By similarity). FT BINDING 192 192 Citrulline (By similarity). FT BINDING 194 194 ATP (By similarity). FT BINDING 201 201 Citrulline (By similarity). FT BINDING 203 203 Citrulline (By similarity). FT BINDING 280 280 Citrulline (By similarity). SQ SEQUENCE 446 AA; 49724 MW; DB3CB1F6F54C217D CRC64; MTTILENLPA GQKVGIAFSG GLDTSAALHW MRIKGAVPYA YTANLGQPDE DDYDAIPKRA IQYGAEGARL IDCRAQLVAE GIAALQCGAF HISTAGVTYF NTTPIGRAVT GTMLVAAMKE DGVNIWGDGS TYKGNDIERF YRYGLLVNPD LKIYKPWLDQ QFIDELGGRA EMSEFMRQAG FEYKMSAEKA YSTDSNLLGA THEAKDLESL ESGIKIVNPI MGVAFWRDDV KIDKEAVTVR FEEGRPVALN GVEYKDAVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL YIAYERLVTG IHNEDTIEQY RENGRRLGRL LYQGRWFDPQ AIMLRETAQR WVARAVTGEV TVELRRGNDY SILATRSPNL TYQPERLSME KVQSTFSPRD RIGQLTMRNL DITDTRDKLR IYSEVGLLTP GESSALPKLK EDESGN //