ID ASTE_PSEAE Reviewed; 332 AA. AC O50177; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 55. DE RecName: Full=Succinylglutamate desuccinylase; DE EC=3.5.1.96; GN Name=astE; Synonyms=aruE; OrderedLocusNames=PA0901; 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: Transforms N(2)-succinylglutamate into succinate and CC glutamate. CC -!- CATALYTIC ACTIVITY: N-succinyl-L-glutamate + H(2)O = succinate + CC L-glutamate. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST CC pathway; L-glutamate and succinate from L-arginine: step 5/5. CC -!- SIMILARITY: Belongs to the aspA/astE family. Succinylglutamate CC desuccinylase 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; AF011922; AAC46014.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04290.1; -; Genomic_DNA. DR PIR; F83533; F83533. DR RefSeq; NP_249592.1; -. DR GeneID; 878165; -. DR GenomeReviews; AE004091_GR; PA0901. DR KEGG; pae:PA0901; -. DR PseudoCAP; PA0901; -. DR HOGENOM; O50177; -. DR OMA; O50177; EKFAIYP. DR BioCyc; PAER208964:PA0901-MON; -. DR BRENDA; 3.5.1.96; 354. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:HAMAP. DR GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP. DR HAMAP; MF_00767; -; 1. DR InterPro; IPR007036; Aste_AspA. DR InterPro; IPR016681; SuccinylGlu_desuccinylase. DR Pfam; PF04952; AstE_AspA; 1. DR PIRSF; PIRSF017020; AstE; 1. DR TIGRFAMs; TIGR03242; arg_catab_astE; 1. PE 3: Inferred from homology; KW Arginine metabolism; Complete proteome; Hydrolase; Metal-binding; KW Zinc. FT CHAIN 1 332 Succinylglutamate desuccinylase. FT /FTId=PRO_0000174643. FT ACT_SITE 215 215 Potential. FT METAL 59 59 Zinc (By similarity). FT METAL 62 62 Zinc (By similarity). FT METAL 151 151 Zinc (By similarity). SQ SEQUENCE 332 AA; 36909 MW; EE8F131836747F59 CRC64; MLALGKLLDL TLAGREPTEK IQLTADGTRL HWLAEGALEV TPIGARDNGV DLLLSAGIHG NETAPIELLE RLIRKVAAGT LKPAARVLFL FGNPEAIRRG ERYVEQDMNR LFNGRHEEGS GNEAFRAAEL ERLAQVFFSK TERVHLHYDL HTAIRGSKIE QFALYPWAEG RQHSRSELAR LRDAGIEAVL LQNKPGITFS AYTYGQLGAE AFTLELGKAR PFGENQEVNL ERLERSLELL IDGSEEQPDG SRLDGLKLFS VSREVIKHSD HFRLHLDDDV ANFTELSPGY LLAEDIGGTR WVVDEVGARI IFPNPRVKNG LRAGILVVPA KL //