ID   ASTE_SHESR              Reviewed;         344 AA.
AC   Q0HVC0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Succinylglutamate desuccinylase {ECO:0000255|HAMAP-Rule:MF_00767};
DE            EC=3.5.1.96 {ECO:0000255|HAMAP-Rule:MF_00767};
GN   Name=astE {ECO:0000255|HAMAP-Rule:MF_00767};
GN   OrderedLocusNames=Shewmr7_1946;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
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., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-succinyl-L-glutamate = L-glutamate + succinate;
CC         Xref=Rhea:RHEA:15169, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:58763; EC=3.5.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00767};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC       {ECO:0000255|HAMAP-Rule:MF_00767}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC       desuccinylase subfamily. {ECO:0000255|HAMAP-Rule:MF_00767}.
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DR   EMBL; CP000444; ABI42935.1; -; Genomic_DNA.
DR   RefSeq; WP_011626142.1; NC_008322.1.
DR   AlphaFoldDB; Q0HVC0; -.
DR   SMR; Q0HVC0; -.
DR   EnsemblBacteria; ABI42935; ABI42935; Shewmr7_1946.
DR   KEGG; shm:Shewmr7_1946; -.
DR   HOGENOM; CLU_071608_0_0_6; -.
DR   OMA; KRYLHSD; -.
DR   OrthoDB; 632656at2; -.
DR   UniPathway; UPA00185; UER00283.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR   GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR   CDD; cd03855; M14_ASTE; 1.
DR   HAMAP; MF_00767; Arg_catab_AstE; 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; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..344
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_0000262083"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ   SEQUENCE   344 AA;  38686 MW;  024A1E812F4E65B9 CRC64;
     MLQALLDSKD FLALTLANPE TLGDEFSFAL GEHTRVEVWD TGVIVFEPAQ 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 VEQEFEAIVF PNAKVPIGNR TVICLIPSVA PDVR