ID   ASTE_SHEDO              Reviewed;         348 AA.
AC   Q12NA7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=Sden_1785;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
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   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-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; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000302; ABE55069.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12NA7; -.
DR   SMR; Q12NA7; -.
DR   STRING; 318161.Sden_1785; -.
DR   KEGG; sdn:Sden_1785; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_071608_0_0_6; -.
DR   OrthoDB; 5290473at2; -.
DR   UniPathway; UPA00185; UER00283.
DR   Proteomes; UP000001982; Chromosome.
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   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00767; Arg_catab_AstE; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR   NCBIfam; TIGR03242; arg_catab_astE; 1.
DR   PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR   PANTHER; PTHR15162:SF7; SUCCINYLGLUTAMATE DESUCCINYLASE; 1.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF017020; AstE; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..348
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_0000262080"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ   SEQUENCE   348 AA;  39197 MW;  3B18928CD9F64240 CRC64;
     MQHELMDNHD FLAFTLAHPH GIAQRFSFEL GQHTQVEVWD TGVIAFLPKE KYTAQAPKQV
     ILSCAVHGNE TAPIEICNRL ITELLTEKVQ AKHRTLFLIG NPPAIHNQTR FIEENMNRLF
     SGAHSKGEGL THAERIRAKA LEDYVAEFYL GAPSNEQRIH YDLHTAIRPS KHEKFAIYPY
     RPGRAYSGEQ IMFLAACGVD TILFHHEPTT TFSYYSSEQF NADAFTVELG KVMPFGQNDM
     SRFEQTQTML TKLVSGEALG LSAFSAEKVN LYKVCRSINK RFEDFAFNFA DQAENFSAFT
     KGEVLATEGG EQVLVEQPQE AIVFPNAKVP VGQRTVLCLV PAPNENIR
//