ID   ASTE_SALDC              Reviewed;         322 AA.
AC   B5FJD4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   02-SEP-2026, entry version 77.
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=SeD_A2039;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-succinyl-L-glutamate + H2O = 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP001144; ACH74276.1; -; Genomic_DNA.
DR   RefSeq; WP_000368464.1; NC_011205.1.
DR   AlphaFoldDB; B5FJD4; -.
DR   SMR; B5FJD4; -.
DR   KEGG; sed:SeD_A2039; -.
DR   HOGENOM; CLU_071608_0_0_6; -.
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   CDD; cd03855; M14_ASTE; 1.
DR   FunFam; 3.40.630.10:FF:000017; Succinylglutamate desuccinylase; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00767; Arg_catab_AstE; 1.
DR   InterPro; IPR050178; AspA/AstE_fam.
DR   InterPro; IPR055438; AstE_AspA_cat.
DR   InterPro; IPR007036; Aste_AspA_hybrid_dom.
DR   InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR   NCBIfam; TIGR03242; arg_catab_astE; 1.
DR   NCBIfam; NF003706; PRK05324.1; 1.
DR   PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR   PANTHER; PTHR15162:SF7; SUCCINYLGLUTAMATE DESUCCINYLASE; 1.
DR   Pfam; PF24827; AstE_AspA_cat; 1.
DR   Pfam; PF04952; AstE_AspA_hybrid; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..322
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_1000133639"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ   SEQUENCE   322 AA;  35634 MW;  E2884FC6C1C232C2 CRC64;
     MDNFLALTLS GTTPRVTQGK SAGFRWRWLG HGLLELTPDA PVDRALILSA GIHGNETAPV
     EMLDKLLSAL FSGSLTLTWR VLVVLGNPQA LAAGIRYCHS DMNRMFGGRW QSFAESDETR
     RARELELSLE TFFSSGHARV RWHLDLHTAI RGSHHLRFGV LPQRDRPWET DFLAWLGAAG
     LEALVFHQAP GGTFTHFSSE HFGALSCALE LGKALPFRQN DLTQFNVTSQ ALSALLSGVE
     TSTSFSPPLR YRVVSQITRH SDKFALYMDA QTLNFTAFAK GTLLAEEGDK RVTVTHDVEY
     VLFPNPSVAC GLRAGLMLER LP
//