ID ASSY_BUCAP Reviewed; 401 AA. AC Q8KA60; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 48. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=argG; OrderedLocusNames=BUsg_047; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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 1 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; AE013218; AAM67618.1; -; Genomic_DNA. DR RefSeq; NP_660407.1; -. DR GeneID; 1005863; -. DR GenomeReviews; AE013218_GR; BUsg_047. DR KEGG; bas:BUsg047; -. DR HOGENOM; Q8KA60; -. DR OMA; Q8KA60; WAARNGR. DR BioCyc; BAPH198804:BUSG047-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_00005; -; 1. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR11587; Arginosuc_synth; 1. 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding. FT CHAIN 1 401 Argininosuccinate synthase. FT /FTId=PRO_0000148577. FT NP_BIND 10 18 ATP (By similarity). FT BINDING 37 37 ATP; via amide nitrogen and carbonyl FT oxygen (By similarity). FT BINDING 89 89 Citrulline (By similarity). FT BINDING 119 119 ATP; via amide nitrogen (By similarity). FT BINDING 121 121 Aspartate (By similarity). FT BINDING 125 125 Aspartate (By similarity). FT BINDING 125 125 Citrulline (By similarity). FT BINDING 126 126 Aspartate (By similarity). FT BINDING 129 129 Citrulline (By similarity). FT BINDING 178 178 Citrulline (By similarity). FT BINDING 187 187 Citrulline (By similarity). FT BINDING 263 263 Citrulline (By similarity). FT BINDING 275 275 Citrulline (By similarity). SQ SEQUENCE 401 AA; 45124 MW; 16DD4B6F98E13D8C CRC64; MNNFKKVVLA YSGGLDTSAI IPWLKENYHV DVVAFVADIG QSKKDLNGIE KKALQSGAID CRVFDLKEEF IKDYVYPVLK TGSLYEGNYL LGTAIARPII AKKQVEFASS IGAKFLCHGA TGKGNDQVRF EIAYAALAPY MKVIAPWREW NLNSRESLLE YLREKNIPTS ATLEKIYSRD ENSLHISTEG GLLEDLWNKP NADCWNWTVE LEDAPEQPEY ISLIVKNGSV VSVNNEFLTP LKCIEKLNKI GSKHAIGRID IVENRLVGIK SRGCYETPGG TIMHIALRAI EQLVFDRESF KWREKIGLEM SSVVYDGRWF TPIRKSLQAS ADSLSSEVNG EVVLKLYKGS VIPVQKKSSN SLYSKEYATF GEDEVYKHSD AEGFIRLFSL SSRIRAQNKL K //