ID ASTB_BURCH Reviewed; 446 AA. AC A0K609; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 16. DE RecName: Full=N-succinylarginine dihydrolase; DE EC=3.5.3.23; GN Name=astB; OrderedLocusNames=Bcen2424_1184; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia RT HI2424."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into CC N(2)-succinylornithine, ammonia and CO(2) (By similarity). CC -!- CATALYTIC ACTIVITY: N(2)-succinyl-L-arginine + 2 H(2)O = N(2)- CC succinyl-L-ornithine + 2 NH(3) + CO(2). CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST CC pathway; L-glutamate and succinate from L-arginine: step 2/5. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family. 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; CP000458; ABK07936.1; -; Genomic_DNA. DR RefSeq; YP_834829.1; -. DR GeneID; 4448252; -. DR GenomeReviews; CP000458_GR; Bcen2424_1184. DR KEGG; bch:Bcen2424_1184; -. DR HOGENOM; A0K609; -. DR OMA; A0K609; HFAHHPA. DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:HAMAP. DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP. DR HAMAP; MF_01172; -; 1. DR InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB. DR Gene3D; G3DSA:3.75.10.20; SuccinylArg_di_hydro; 1. DR Pfam; PF04996; AstB; 1. DR TIGRFAMs; TIGR03241; arg_catab_astB; 1. PE 3: Inferred from homology; KW Arginine metabolism; Complete proteome; Hydrolase. FT CHAIN 1 446 N-succinylarginine dihydrolase. FT /FTId=PRO_1000065714. FT REGION 19 28 Substrate binding (By similarity). FT REGION 137 138 Substrate binding (By similarity). FT ACT_SITE 174 174 By similarity. FT ACT_SITE 249 249 By similarity. FT ACT_SITE 370 370 Nucleophile (By similarity). FT BINDING 110 110 Substrate (By similarity). FT BINDING 213 213 Substrate (By similarity). FT BINDING 251 251 Substrate (By similarity). FT BINDING 364 364 Substrate (By similarity). SQ SEQUENCE 446 AA; 48327 MW; 15E1E87E4AB138B7 CRC64; MNAQEANFDG LVGPTHNYAG LSFGNVASLN NEKSAANPKA AAKQGLRKMK QLADLGFAQG VLPPQERPSL RLLRELGFSG KDADVIAKAA KQAPELLAAA SSASAMWTAN AATVSPSADT SDGRVHFTPA NLCSKLHRAI EHEATRRTLS TLFADPTHFA VHEALTGTPA LGDEGAANHT RFCAEYGKPG IEFFVYGRAE YRRGPEPKRF PARQTFEASR AVAHRHGLAE EATVYAQQDP DVIDAGVFHN DVISVGNRDT LFTHERAFVN KQAIYDTLTA ALDARGARLN VIEVPDAAVS VNDAVTSYLF NSQLLSRADG SQVLVVPQEC RENARVAAYL DQLAAGNGPI HDVLVFDLRE SMKNGGGPAC LRLRVVLNDA ERAAVTSNVW INDTLFASLD AWIDKHYRDR LAPEDLADPA LLDESRTALD ELTQILRVGS LYDFQR //