ID ASTE_SHESM Reviewed; 344 AA. AC Q0HIL5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Succinylglutamate desuccinylase; DE EC=3.5.1.96; GN Name=astE; OrderedLocusNames=Shewmr4_2029; OS Shewanella sp. (strain MR-4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=60480; 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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., RA Tiedje J., Richardson P.; RT "Complete sequence of Shewanella sp. MR-4."; RL Submitted (AUG-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; CP000446; ABI39102.1; -; Genomic_DNA. DR RefSeq; YP_734159.1; -. DR GeneID; 4252602; -. DR GenomeReviews; CP000446_GR; Shewmr4_2029. DR KEGG; she:Shewmr4_2029; -. DR HOGENOM; Q0HIL5; -. DR OMA; Q0HIL5; 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 1 344 Succinylglutamate desuccinylase. FT /FTId=PRO_0000262082. FT ACT_SITE 224 224 Potential. FT METAL 63 63 Zinc (By similarity). FT METAL 66 66 Zinc (By similarity). FT METAL 160 160 Zinc (By similarity). SQ SEQUENCE 344 AA; 38716 MW; EB013EF7E444C9B6 CRC64; MLQALLDSKD FLALTLANPE TLGDEFSFTL GEHTRVEVWD TGVIVFEPVQ AQGKDVILSC GVHGNETAPI ELCNTLIKQL LQQKIIAKQR TLFLIGNPLA INNGTRIIDE NMNRLFSGEH SNPPGLVNPE RVRAKKLEAY VDRFFKGAAA GRQRIHYDLH TAMRASKHEK FAIYPYRPGR AYSAEQIMFL AASGVDTVLF HHEPTTTFSY FSSEQYGADA FTIELGKVYP MGQNDMTRFI AAQEMFMRLI TDKPLALEPF SADKVNLYQV CRVINKHFDD FEFTFATDVE NFRSFPKGFV LAREGGQEIK VEQECESIVF PNAKVPIGNR TVICLIPSVA PDVR //