ID ASTB_PSEAE Reviewed; 448 AA. AC O50175; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 52. DE RecName: Full=N-succinylarginine dihydrolase; DE EC=3.5.3.23; GN Name=astB; Synonyms=aruB; OrderedLocusNames=PA0899; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=98053840; PubMed=9393691; RA Itoh Y.; RT "Cloning and characterization of the aru genes encoding enzymes of the RT catabolic arginine succinyltransferase pathway in Pseudomonas RT aeruginosa."; RL J. Bacteriol. 179:7280-7290(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into CC N(2)-succinylornithine, ammonia and CO(2). 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; AF011922; AAC46013.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04288.1; -; Genomic_DNA. DR PIR; D83533; D83533. DR RefSeq; NP_249590.1; -. DR GeneID; 878588; -. DR GenomeReviews; AE004091_GR; PA0899. DR KEGG; pae:PA0899; -. DR PseudoCAP; PA0899; -. DR HOGENOM; O50175; -. DR OMA; O50175; KMKALME. DR BioCyc; PAER208964:PA0899-MON; -. DR BRENDA; 3.5.3.23; 354. 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 1 448 N-succinylarginine dihydrolase. FT /FTId=PRO_0000064716. 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 250 250 By similarity. FT ACT_SITE 371 371 Nucleophile (By similarity). FT BINDING 110 110 Substrate (By similarity). FT BINDING 214 214 Substrate (By similarity). FT BINDING 252 252 Substrate (By similarity). FT BINDING 365 365 Substrate (By similarity). SQ SEQUENCE 448 AA; 48875 MW; 39F9F379CCC16196 CRC64; MNAHEVNFDG LVGPTHNYGG LSYGNVASQS NSQAVSNPKE AAKQGLAKMK ALMEMGFKQG VLAPQARPDT AALRSLGFSG SDEEVIRRAA KEAMPLLAAC SSASSMWTAN AATVSPSADT ADGRVHFTAA NLNCKFHRSI EHPTTSRVLA AMFNDERHFA HHAALPAVSQ FGDEGAANHT RFCKDYGDAG VEFFVFGRSA FDSRFPAPQR YPARQTLEAC QAVARLHGLS EAGVVYAQQN PAVIDQGVFH NDVISVGNGE VLFHHEDAFL DTEKVLAELH DKLGRRGGRF RAICVPRDQV AVEDAVKSYL FNSQLLSKAD GSMLLVVPEE CRNNPRVWNY LDQLTGDDGP IREVKVFDLK QSMQNGGGPA CLRLRVALQE RELAAVNPGV IMSAGLYDTL VAWVDRHYRD RLSETDLADP QLLLECRTAL DELTQILKLG SVYSFQLD //