ID A0A2A2IWA5_9PSED Unreviewed; 332 AA.
AC A0A2A2IWA5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ECO:0000313|EMBL:PAV48784.1};
GN ORFNames=CK486_05105 {ECO:0000313|EMBL:PAV48784.1};
OS Pseudomonas sp. HAR-UPW-AIA-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1985301 {ECO:0000313|EMBL:PAV48784.1, ECO:0000313|Proteomes:UP000243299};
RN [1] {ECO:0000313|Proteomes:UP000243299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAR-UPW-AIA-41 {ECO:0000313|Proteomes:UP000243299};
RA Kumari P., Krishnamurthi S.;
RL Submitted (SEP-2017) 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:PAV48784.1}.
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DR EMBL; NSLB01000002; PAV48784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2IWA5; -.
DR OrthoDB; 5290473at2; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000243299; 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:UP000243299};
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 332 AA; 36381 MW; F8C4324D8989EFAB CRC64;
MLSLGKLLDL TLAGREPTEK IQLTAAGVRL HWLAEGALEV SPIKSEDAGL DLLLSAGLHG
NETAPIELLD RLLQAIASGE LRPRVRILFL LGNPEAMRRG ERYVEQDINR LFSGRHEAAS
GFEALRAGEL EQLAANFFSL AGRERLHYDL HTAIRGSQIE QFALYPYRDG CQHSARQLAR
LRDAGIGAVL LQNKTGITFS SHTYAHLQAE AFTLELGKAR PFGENQGVNL MRLEAVLRDL
IANGSSGDDE DFSGLQLFVV AREVIKHSDG FQLHLAPDVE NFTALPKGFL LAEDIAGSRW
LIEEEGARII FPNPKVKNGL RAGIIVVPAV SL
//
