ID A0A071LWZ3_9ENTR Unreviewed; 326 AA.
AC A0A071LWZ3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=DT73_12020 {ECO:0000313|EMBL:KEA52810.1};
OS Mangrovibacter sp. MFB070.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Mangrovibacter.
OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA52810.1, ECO:0000313|Proteomes:UP000027726};
RN [1] {ECO:0000313|EMBL:KEA52810.1, ECO:0000313|Proteomes:UP000027726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA52810.1,
RC ECO:0000313|Proteomes:UP000027726};
RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT Bacterium Isolated from an Aquaculture Farm.";
RL Submitted (APR-2014) 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:KEA52810.1}.
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DR EMBL; JJMI01000022; KEA52810.1; -; Genomic_DNA.
DR RefSeq; WP_036108504.1; NZ_JJMI01000022.1.
DR AlphaFoldDB; A0A071LWZ3; -.
DR eggNOG; COG2988; Bacteria.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000027726; 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:UP000027726};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00767}.
FT ACT_SITE 209
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 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
SQ SEQUENCE 326 AA; 35915 MW; 7C49E9A9BFFF8914 CRC64;
MDEFVQTTLA GLVPAQKKGE GPGFRWQWLE QGVIRLTPHS KVTRSLVLSA GIHGNETAPV
EILSQVLDAL WSGEIALCWD VLVVLGNPLA LQTGKRYQAC DLNRMFGGRW EAFEPGTERA
RAELLEQVVG GFFENSPPVR WHLDMHTAIR GSLHPRFGVL PARNAAWPAA FLQWLEMAGL
EALVFHQTPG GTFTHFTAQY YDALSCTMEL GKAMPFGQNN LNAFSAARHA LGELLGKGPE
AVPVVQQPVA RCYKVSQQLT RTGEAFILHI PDDTVNFTPF SKGELLAEDG DNKQVVQQET
EYVLFPNRLV APGLRAGLML AEIPHP
//
