ID   ASTE_SHEON              Reviewed;         344 AA.
AC   Q8EEN9;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=Succinylglutamate desuccinylase;
DE            EC=3.5.1.96;
GN   Name=astE; OrderedLocusNames=SO_2338;
OS   Shewanella oneidensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=70863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A.,
RA   Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S.,
RA   Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A.,
RA   White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M.,
RA   Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O.,
RA   Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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.
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DR   EMBL; AE014299; AAN55372.1; -; Genomic_DNA.
DR   RefSeq; NP_717928.1; -.
DR   GeneID; 1170061; -.
DR   GenomeReviews; AE014299_GR; SO_2338.
DR   KEGG; son:SO_2338; -.
DR   NMPDR; fig|211586.1.peg.2117; -.
DR   TIGR; SO_2338; -.
DR   HOGENOM; Q8EEN9; -.
DR   OMA; Q8EEN9; EKFAIYP.
DR   BioCyc; SONE211586:SO_2338-MON; -.
DR   BRENDA; 3.5.1.96; 257422.
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_0000174648.
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;  38783 MW;  0ECF6CEA903B21F7 CRC64;
     MLQALLDSKD FLALTLANPQ TLGDEFSFTL GEHTRVNVWD TGVIVFEPAQ PQGKDVILSC
     GVHGNETAPI ELCNTLIKQL LQQKIIAKQR TLFLIGNPLA INNGTRIIDE NMNRLFSGEH
     SNPPGLVNPE RLRAKKLETY VDRFFKAAAA GRQRIHYDLH TAMRASKHEK FAIYPYRPGR
     AYSAEQIMFL AASGVDTVLF HHEPTTTFSY FSSEQYGADA FTIELGKVYP MGQNDMTRFI
     AAQEMFTRLI TDKPLQLESF STDKVNLYQV CRVINKHFDD FEFTFATDVE NFRAFPKGFV
     LAREGGQEIK VEQEVESIVF PNAKVPIGNR TVICLIPSVA PDVR
//