ID ASTE_ECOL6 Reviewed; 322 AA. AC Q8FH03; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 39. DE RecName: Full=Succinylglutamate desuccinylase; DE EC=3.5.1.96; GN Name=astE; OrderedLocusNames=c2144; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). 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; AE014075; AAN80603.1; -; Genomic_DNA. DR RefSeq; NP_754038.1; -. DR SMR; Q8FH03; 1-322. DR GeneID; 1036569; -. DR GenomeReviews; AE014075_GR; c2144. DR KEGG; ecc:c2144; -. DR HOGENOM; Q8FH03; -. DR OMA; Q8FH03; EKFAIYP. DR BRENDA; 3.5.1.96; 292881. 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 1 322 Succinylglutamate desuccinylase. FT /FTId=PRO_0000174641. 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 322 AA; 35855 MW; 500A2B5E5E302454 CRC64; MDNFLALTLT GKKPVITERE INGVRWRWLG DGVLELTPLT PPQGVLVISA GIHGNETAPV EMLDALLGAI SHGEIPLRWR LLVILGNPPA LKQGKRYCHS DMNRMFGGRW QLFAESGETC RARELEQCLE DFYDQGKESV RWHLDLHTAI RGSLHPQFGV LPQRDIPWDE KFLTWLGAAG LEALVFHQEP GGTFTHFSAR HFGALACTLE LGKALPFGQN DLRQFAVTAS AIAALLSGES VGIVRTPPLR YRVVSQITRH SPSFEMHMAN DTLNFMPFEK GTLLAQDGEE RFTVTHDVEY VLFPNPLVAL GLRAGLMLEK IS //