ID ASTB_ECOK1 Reviewed; 447 AA. AC A1ABS6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 16-JUN-2009, entry version 17. DE RecName: Full=N-succinylarginine dihydrolase; DE EC=3.5.3.23; GN Name=astB; OrderedLocusNames=Ecok1_16220; ORFNames=APECO1_814; OS Escherichia coli O1:K1 / APEC. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=405955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17293413; DOI=10.1128/JB.01726-06; RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., RA Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., RA Nolan L.K.; RT "The genome sequence of avian pathogenic Escherichia coli strain RT O1:K1:H7 shares strong similarities with human extraintestinal RT pathogenic E. coli genomes."; RL J. Bacteriol. 189:3228-3236(2007). 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; CP000468; ABJ01116.1; -; Genomic_DNA. DR RefSeq; YP_852830.1; -. DR SMR; A1ABS6; 2-441. DR GeneID; 4495253; -. DR GenomeReviews; CP000468_GR; Ecok1_16220. DR KEGG; ecv:APECO1_814; -. DR OMA; A1ABS6; 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 1 447 N-succinylarginine dihydrolase. FT /FTId=PRO_1000065725. 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 248 248 By similarity. FT ACT_SITE 365 365 Nucleophile (By similarity). FT BINDING 110 110 Substrate (By similarity). FT BINDING 212 212 Substrate (By similarity). FT BINDING 250 250 Substrate (By similarity). FT BINDING 359 359 Substrate (By similarity). SQ SEQUENCE 447 AA; 49539 MW; D0A508A29B8B66FD CRC64; MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK KLADAGFPQA VIPPHERPFI PVLRQLGFRG SDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATIAPSADT LDGKVHLTVA NLNNKFHRSL EAPVTESLLK AIFNDEEKFS VHSALPQVAL LGDEGAANHN RLGGHYGEPG MQLFVYGREE GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD VIDQGVFHND VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVFVSDAV STYLFNSQLL SRDDGSMVLV LPQECREHAG VWRYLNELLA ADNPISELKV FDLRESMANG GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR YYRDRLTAAD LADPQLLREG REALDTLTQL LDLGSVYPFQ REGGGNG //