ID   ASTE_PSEP1              Reviewed;         335 AA.
AC   A5W0D8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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}; OrderedLocusNames=Pput_1440;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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; CP000712; ABQ77598.1; -; Genomic_DNA.
DR   RefSeq; WP_012051581.1; NC_009512.1.
DR   AlphaFoldDB; A5W0D8; -.
DR   SMR; A5W0D8; -.
DR   STRING; 351746.Pput_1440; -.
DR   EnsemblBacteria; ABQ77598; ABQ77598; Pput_1440.
DR   KEGG; ppf:Pput_1440; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_071608_0_0_6; -.
DR   OMA; FIIAHPE; -.
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..335
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_1000017326"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ   SEQUENCE   335 AA;  37451 MW;  D423F185B35FBA9F CRC64;
     MLALGKLLEL TLTAHEPAEK TQVTPGGARL RWLGEGALEV RPAESEDCGL DLLLSAGIHG
     NETAPIELLE RLLHGVANGK IKPRARVLFL FGNPAAIRKG ERFIEQDINR LFNGRHELSS
     GFEALRAAEL EQFARVFFSK PGRNRLHYDL HTAIRGSKIE QFALYPYKEG RKHSRRELAR
     LAAAGMEAVL LQSKSSITFS AFTYEQLEAE AFTLELGKAR PFGQNEQVNL DKLEERLIRI
     IEATEPENES SLDGLQLFSV SREIIKHSDS FHLHLPADIE NFSELSKGYL LAEDLAEMRW
     VVEEEGARII FPNPKVKNGL RAGILIVPDS GQRLG