ID ASTE_YERE8 Reviewed; 330 AA. AC A1JS32; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Succinylglutamate desuccinylase; DE EC=3.5.1.96; GN Name=astE; OrderedLocusNames=YE2465; OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=393305; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206; RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J., RA Prentice M.B.; RT "The complete genome sequence and comparative genome analysis of the RT high pathogenicity Yersinia enterocolitica strain 8081."; RL PLoS Genet. 2:2039-2051(2006). CC -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and CC glutamate (By similarity). 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; AM286415; CAL12508.1; -; Genomic_DNA. DR RefSeq; YP_001006672.1; -. DR GeneID; 4712503; -. DR GenomeReviews; AM286415_GR; YE2465. DR KEGG; yen:YE2465; -. DR NMPDR; fig|630.2.peg.2388; -. DR OMA; A1JS32; EKFAIYP. 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 1 330 Succinylglutamate desuccinylase. FT /FTId=PRO_1000017334. FT ACT_SITE 210 210 Potential. FT METAL 53 53 Zinc (By similarity). FT METAL 56 56 Zinc (By similarity). FT METAL 147 147 Zinc (By similarity). SQ SEQUENCE 330 AA; 36775 MW; B86527782F6E931B CRC64; MPDFLSITLS GVPPSLTSGE TSNLKWQWVD EGVLMLTPHG ACSQSVVLSA GIHGNETAPI EILNQLVSDL LASQLPLAVR LLVILGNPPA IRAGERYLTA DINRMFGGRY KNHSLTDEAR RAEILEQKVG EFFASDPLSL RLHYDLHTAI RGSHHNRFGL LPYRTTPYCA AMLRWLKDSE LDALVMHTSA GGTFAHFSSE FCQAASCTLE LGKALPFGQN QLEQFRPITA GLRALVSGGQ LPTRSTEAMI FYRVVKSLLK QHADFKLWVA DDTVNFTRYP QGTLMIEQLN EHYCVEHEYE WILFPNPRVA LGLRAGIMLV QMDENDLLQA //