ID A0A2G8TKB4_9BURK Unreviewed; 327 AA.
AC A0A2G8TKB4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=CR105_05365 {ECO:0000313|EMBL:PIL46490.1};
OS Massilia eurypsychrophila.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1485217 {ECO:0000313|EMBL:PIL46490.1, ECO:0000313|Proteomes:UP000230390};
RN [1] {ECO:0000313|EMBL:PIL46490.1, ECO:0000313|Proteomes:UP000230390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30074 {ECO:0000313|EMBL:PIL46490.1,
RC ECO:0000313|Proteomes:UP000230390};
RA Wang H.;
RT "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL Submitted (OCT-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:PIL46490.1}.
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DR EMBL; PDOC01000002; PIL46490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8TKB4; -.
DR OrthoDB; 5290473at2; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000230390; 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 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:UP000230390};
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 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00767"
FT BINDING 61
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 327 AA; 34257 MW; A5A83B578E7B1EE7 CRC64;
METVPPAVRQ LASADFSELA RRFEQAGFAV TMPAAGIVTL KAPPGGMRTS VLVSVGVHGD
ETGPIEVLAH VLDALSRQPA ALAVDLMVCV GNIDAIAAGK RFIDADLNRM FRAQRGSLAG
AAEAARADVM VQATADFFAG AGPVRWHLDL HTAIRPSEYP TFAVVPELIA DGPKAALIEW
LGQAAIGAII LNPQSAGTYS YYSAEHHGAA ASTVELGRVG TLGQNDLSQF ADVDRALAGL
LRGADLPAAA AAPHVFKVAQ EIIKLSDDFK MAFGRETRNF TALAAGAVIA TDGDTTYRVQ
HAQELVVFPN PDVRVGLRAG LMVVRSA
//
