ID   ASTE_SALTY              Reviewed;         322 AA.
AC   Q8ZPU8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=STM1307;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   INDUCTION.
RX   PubMed=10074092; DOI=10.1128/jb.181.6.1934-1938.1999;
RA   Lu C.-D., Abdelal A.T.;
RT   "Role of ArgR in activation of the ast operon, encoding enzymes of the
RT   arginine succinyltransferase pathway in Salmonella typhimurium.";
RL   J. Bacteriol. 181:1934-1938(1999).
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   -!- INDUCTION: By nitrogen and carbon starvation, and arginine, via the
CC       ArgR and Crp transcriptional regulators. {ECO:0000269|PubMed:10074092}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC       desuccinylase subfamily. {ECO:0000255|HAMAP-Rule:MF_00767}.
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DR   EMBL; AE006468; AAL20232.1; -; Genomic_DNA.
DR   RefSeq; NP_460273.1; NC_003197.2.
DR   RefSeq; WP_000368454.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPU8; -.
DR   SMR; Q8ZPU8; -.
DR   STRING; 99287.STM1307; -.
DR   PaxDb; Q8ZPU8; -.
DR   EnsemblBacteria; AAL20232; AAL20232; STM1307.
DR   GeneID; 1252825; -.
DR   KEGG; stm:STM1307; -.
DR   PATRIC; fig|99287.12.peg.1389; -.
DR   HOGENOM; CLU_071608_0_0_6; -.
DR   OMA; KRYLHSD; -.
DR   PhylomeDB; Q8ZPU8; -.
DR   BioCyc; SENT99287:STM1307-MON; -.
DR   UniPathway; UPA00185; UER00283.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Arginine metabolism; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..322
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_0000174647"
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;  35641 MW;  38A4CBBE972C5E8A CRC64;
     MDNFLALTLS GTTPRVTQGK GAGFRWRWLG HGLLELTPDA PVDRALILSA GIHGNETAPV
     EMLDKLLSAL YSGSLTLTWR VLVVLGNPQA LAAGIRYCHS DMNRMFGGRW QSFAESDETR
     RARELELSLE TFFSSGQARV RWHLDLHTAI RGSHHLRFGV LPQRDRPWET DFLAWLGAAG
     LEALVFHQAP GGTFTHFSSE HFGALSCTLE LGKALPFRQN DLTQFNVTSQ ALSALLSGVE
     TSTSFSPPLR YRVVSQITRH SDKFALYMDA QTLNFTAFAK GTLLAEEGDK RVTVTHDVEY
     VLFPNPSVAC GLRAGLMLER LP