ID A0A1I3P5M5_9PSED Unreviewed; 336 AA.
AC A0A1I3P5M5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05216206_3588 {ECO:0000313|EMBL:SFJ16848.1};
OS Pseudomonas guineae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=425504 {ECO:0000313|EMBL:SFJ16848.1, ECO:0000313|Proteomes:UP000243606};
RN [1] {ECO:0000313|Proteomes:UP000243606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24016 {ECO:0000313|Proteomes:UP000243606};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOQL01000006; SFJ16848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3P5M5; -.
DR STRING; 425504.SAMN05216206_3588; -.
DR OrthoDB; 5290473at2; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000243606; 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 PIRSF; PIRSF017020; AstE; 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:UP000243606};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00767}.
FT ACT_SITE 215
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
SQ SEQUENCE 336 AA; 37389 MW; C9B672DD44D0DFCF CRC64;
MLALGKLLEL TLAGHEPAAK IQLTPEGTRL RWLAEGALEV TPPAARDNGQ DLLFSAGIHG
NETAPIELLD RLLQGIARNQ LQPQARILFL FGNTAAMRRG ERYIEQDINR LFNGRHDQHS
GAEALRACEL EHLAAAFFSK PERTRLHYDL HTAIRASKIE QFALYPFQDG RPRSQRELSR
LNAAGIEAVL LHNKSSVTFS AFTYSQLGAE ALTLELGKAR PFGQNERVNL DRLELHLQAL
IEGRELEGAT DDLGELKLFA VAREVIKHSD AFQLHLPADV ENFSELPVGY LLAEDLSDTR
WVIDEPGTRI IFPNPKVKNG LRAGILIVPA EDVQLI
//
