ASTE_SALTI
ID ASTE_SALTI Reviewed; 322 AA.
AC Q8Z6G3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=STY1807, t1186;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD02047.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68842.1; -; Genomic_DNA.
DR RefSeq; NP_456205.1; NC_003198.1.
DR RefSeq; WP_000368452.1; NZ_WSUR01000034.1.
DR AlphaFoldDB; Q8Z6G3; -.
DR SMR; Q8Z6G3; -.
DR STRING; 220341.16502884; -.
DR EnsemblBacteria; AAO68842; AAO68842; t1186.
DR KEGG; stt:t1186; -.
DR KEGG; sty:STY1807; -.
DR PATRIC; fig|220341.7.peg.1819; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_071608_0_0_6; -.
DR OMA; KRYLHSD; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 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..322
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_0000174646"
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; 35474 MW; 59B13171DCCCA53A CRC64;
MDNFLALTLS GTTPRVTQGK GAGFRWRWLG HGLLELTPDA PVDRALILSA GIHGNETAPV
EMLDKLLSAL YSGSLTLTWR VLVVLGNPQA LAAGIRYCHS DMNRMFGGRW QSFAESDETR
RARELELSLE TFFSSGQARV RWHLDLHTAI RGSHHLRFGV LPQRDRPWEA DFLAWLGAAG
LEALVFHQAP GGTFTHFSSE HFGALSCTLE LGKALPFGQN DLTQFSVTSQ ALSALLSGVE
TSTSFSPPLR YRVVSQITRH SDKFALYMDA QTLNFTAFAK GTLLAEEGDK RVTVTHDVEY
VLFPNSSVAC GLRAGLMLER LP
