ID ASSY_ANAVT Reviewed; 400 AA. AC Q3MBE6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Argininosuccinate synthase; DE EC=6.3.4.5; DE AltName: Full=Citrulline--aspartate ligase; GN Name=argG; OrderedLocusNames=Ava_2068; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-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 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; CP000117; ABA21690.1; -; Genomic_DNA. DR RefSeq; YP_322585.1; -. DR GeneID; 3680541; -. DR GenomeReviews; CP000117_GR; Ava_2068. DR KEGG; ava:Ava_2068; -. DR NMPDR; fig|240292.3.peg.1347; -. DR HOGENOM; Q3MBE6; -. DR OMA; Q3MBE6; IAPVREW. DR BioCyc; AVAR240292:AVA_2068-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 1 400 Argininosuccinate synthase. FT /FTId=PRO_0000263906. FT NP_BIND 10 18 ATP (By similarity). FT BINDING 38 38 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 177 177 Citrulline (By similarity). FT BINDING 186 186 Citrulline (By similarity). FT BINDING 262 262 Citrulline (By similarity). FT BINDING 274 274 Citrulline (By similarity). SQ SEQUENCE 400 AA; 43959 MW; 720C4C6C608EF417 CRC64; MGRAKKVVLA YSGGVDTSVC IPYLKQEWGV EEVITLAADL GQGDELEPIR EKALKSGASE SLVADVKESF IKDYAFPAIQ ANALYENRYP LGTALARPLI AKILVEAAEK YGADAIAHGC TGKGNDQVRF DVSCTALNPK LKILAPAREW GMSREATIAY GEKFGIPSPV KKSSPYSIDK NLLGRSIEAG ALEDPKFEPP EEIYEMTKAI ADTPNEPEYI EIGFTQGLPT TINGTPKDPV ALIQELNQLV GSHGVGRIDM IENRLVGIKS REIYESPAML VLIQAHRDLE SLTLTADVSH YKRGIEETYS QIVYNGLWYS PLKAALDAFI QKTQERVSGI VRVKLFKGNA TIVGRWSDSS LYTPDLATYG AEDQFDHKAA EGFIYVWGLP TRIWAQQDRG //