ID ASTE_PSEA6 Reviewed; 350 AA. AC Q15TS5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Succinylglutamate desuccinylase; DE EC=3.5.1.96; GN Name=astE; OrderedLocusNames=Patl_2195; OS Pseudoalteromonas atlantica (strain T6c / BAA-1087). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=342610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.; RT "Complete sequence of Pseudoalteromonas atlantica T6c."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000388; ABG40713.1; -; Genomic_DNA. DR RefSeq; YP_661767.1; -. DR GeneID; 4172347; -. DR GenomeReviews; CP000388_GR; Patl_2195. DR KEGG; pat:Patl_2195; -. DR NMPDR; fig|342610.3.peg.3166; -. DR HOGENOM; Q15TS5; -. DR OMA; Q15TS5; EKFAIYP. DR BioCyc; PATL342610:PATL_2195-MON; -. 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 1 350 Succinylglutamate desuccinylase. FT /FTId=PRO_0000262079. FT ACT_SITE 233 233 Potential. FT METAL 71 71 Zinc (By similarity). FT METAL 74 74 Zinc (By similarity). FT METAL 169 169 Zinc (By similarity). SQ SEQUENCE 350 AA; 39246 MW; 9B68EB60E9BA6BC4 CRC64; MQTVNTHKLI SHLQQQGQFL TLSRCSGELV QNPISFTLYE HTQVSIISPG IISFSPKIKS DKAIVLSSGI HGNETAPIEI CDQYVIDILT GKIRVAHRIL FIFGNLPAMD RATRFVDENL NRLFSHAHAS ESVDQNSYEC ARAKEIEEAV AEFYGSGHGE ESRYHYDLHT AIRPSKNEKF AVYPFLHGEK HDKEQISFLL ACGIDTFLLS GSPTTTFSYY SSRQFGAHAF TVELGKVQAF GQNDMSRFTQ VNDTLKRFIS GQPLNLKSFN DQDVLIYQVN QVINKHAEDF ELDFSDDLPN FSDFPKGTLL AHETGNEYRA EFDGEAVVFP NANVAIGQRA ILTVIPTTLD //