ID ARLY_BRUC2 Reviewed; 466 AA. AC A9M968; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 16-JUN-2009, entry version 11. DE RecName: Full=Argininosuccinate lyase; DE Short=ASAL; DE EC=4.3.2.1; DE AltName: Full=Arginosuccinase; GN Name=argH; OrderedLocusNames=BCAN_A2026; OS Brucella canis (strain ATCC 23365 / NCTC 10854). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=483179; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate + CC L-arginine. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 3/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC 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; CP000872; ABX63015.1; -; Genomic_DNA. DR RefSeq; YP_001593786.1; -. DR GeneID; 5783924; -. DR GenomeReviews; CP000872_GR; BCAN_A2026. DR KEGG; bcs:BCAN_A2026; -. DR OMA; A9M968; ATDTRLY. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:HAMAP. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro. DR HAMAP; MF_00006; -; 1. DR InterPro; IPR009049; Argininosuccinate_lyase. DR InterPro; IPR003031; D_crystallin. DR InterPro; IPR000362; Fumarate_lyase. DR PANTHER; PTHR11444:SF3; argH; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00145; DCRYSTALLIN. DR PRINTS; PR00149; FUMRATELYASE. DR TIGRFAMs; TIGR00838; argH; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; Lyase. FT CHAIN 1 466 Argininosuccinate lyase. FT /FTId=PRO_1000073838. SQ SEQUENCE 466 AA; 51285 MW; CE957213BDE31D32 CRC64; MSEQKSSNQM WGGRFASGPD AIMEEINASI GFDRKLYAQD IQGSLAHAAM LAKTGIIAAE DHKQIENGLK TIRKEIEEGK FTFSRKLEDI HMNIEARLAE LIGPAAGRLH TARSRNDQVA VDFRLWVKQE LEKTAAALKN LIEAFLERAE EHAATVMPGF THLQTAQPVT FGHHCMAYVE MFGRDLSRVR DAIERMDESP LGAAALAGTG FPIDRHMTAK ALGFREPTRN SLDSVSDRDY ALEFLSLAAI CAGHLSRLAE EIVIWSTPQF NFVRLSDAFS TGSSIMPQKK NPDAAELVRA KTGRINGSLV ALLTIMKGLP LAYSKDMQED KEQVFDAAEN LELAIAAMAG MVRDLTVNVA AMKKAAGSGY STATDLADWL VRTLGLPFRE AHHVTGRAVA LAESRKVDLA KLSLEELQSI NPAITAEVFG YLTVEKSVKS RQSFGGTAPQ EVRRQIRYWK KRIAKA //