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Database: UniProt
Entry: A0A3N1J295_9ENTR
LinkDB: A0A3N1J295_9ENTR
Original site: A0A3N1J295_9ENTR 
ID   A0A3N1J295_9ENTR        Unreviewed;       324 AA.
AC   A0A3N1J295;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Succinylglutamate desuccinylase {ECO:0000256|HAMAP-Rule:MF_00767};
DE            EC=3.5.1.96 {ECO:0000256|HAMAP-Rule:MF_00767};
GN   Name=astE {ECO:0000256|HAMAP-Rule:MF_00767};
GN   ORFNames=EDF81_0116 {ECO:0000313|EMBL:ROP61644.1};
OS   Enterobacter sp. BIGb0383.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=2485118 {ECO:0000313|EMBL:ROP61644.1, ECO:0000313|Proteomes:UP000280899};
RN   [1] {ECO:0000313|EMBL:ROP61644.1, ECO:0000313|Proteomes:UP000280899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIGb0383 {ECO:0000313|EMBL:ROP61644.1,
RC   ECO:0000313|Proteomes:UP000280899};
RA   Samuel B.;
RT   "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00767};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00767};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00767}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC       desuccinylase subfamily. {ECO:0000256|HAMAP-Rule:MF_00767}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROP61644.1}.
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DR   EMBL; RJKQ01000001; ROP61644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1J295; -.
DR   UniPathway; UPA00185; UER00283.
DR   Proteomes; UP000280899; Unassembled WGS sequence.
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   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism {ECO:0000256|ARBA:ARBA00022503, ECO:0000256|HAMAP-
KW   Rule:MF_00767};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00767};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00767}; Reference proteome {ECO:0000313|Proteomes:UP000280899};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00767}.
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
SQ   SEQUENCE   324 AA;  36255 MW;  8CAC0AB3C14AC804 CRC64;
     MENFLALTLT GVAPHPLSGE TAQFHWQWLE EGVLLLIPHQ PAEGSLVLSA AVHGNETAPV
     EMVDRLLSAL FAGTQPLHLR LLVIFGNPLA MRAGKRHLQH DMNRMFGERW QQYPPCEETA
     RAARLEAHVG HFFAPESDGP RWHLDLHTAI RGSLHPRFGV LPARQSPWDE GFLNWLGSAG
     LEALVFHQSP GGTFSHFSAE RFSALSCTLE LGKALPFGHN DLHQFATTQL ALAALLAGEM
     ERRAVTAPIR YRVVQQLTRS SEDFRLHMSD DTLNFTPFCA GTLLAEEGER RWVVEKAWEF
     VLFPNPNVAV GLRAGLMLEK WQEE
//
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