ID   ASTE_VIBC3              Reviewed;         342 AA.
AC   A5F1U8; C3M003;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Succinylglutamate desuccinylase {ECO:0000255|HAMAP-Rule:MF_00767};
DE            EC=3.5.1.96 {ECO:0000255|HAMAP-Rule:MF_00767};
GN   Name=astE {ECO:0000255|HAMAP-Rule:MF_00767};
GN   OrderedLocusNames=VC0395_A0863, VC395_1361;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC       glutamate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00767};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00767}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC       desuccinylase subfamily. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000627; ABQ19642.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP09369.1; -; Genomic_DNA.
DR   RefSeq; WP_000167428.1; NZ_JAACZH010000002.1.
DR   AlphaFoldDB; A5F1U8; -.
DR   SMR; A5F1U8; -.
DR   STRING; 345073.VC395_1361; -.
DR   EnsemblBacteria; ABQ19642; ABQ19642; VC0395_A0863.
DR   KEGG; vco:VC0395_A0863; -.
DR   KEGG; vcr:VC395_1361; -.
DR   PATRIC; fig|345073.21.peg.1322; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_071608_0_0_6; -.
DR   OMA; FIIAHPE; -.
DR   UniPathway; UPA00185; UER00283.
DR   Proteomes; UP000000249; Chromosome 2.
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   HAMAP; MF_00767; Arg_catab_AstE; 1.
DR   InterPro; IPR007036; Aste_AspA.
DR   InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF017020; AstE; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..342
FT                   /note="Succinylglutamate desuccinylase"
FT                   /id="PRO_1000072833"
FT   ACT_SITE        219
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
SQ   SEQUENCE   342 AA;  39033 MW;  F5B2C58B0842239E CRC64;
     MTKSLFRQSF LFDSLDLDHP MVAQTVRTEQ GVTLKLHQRG VLEVIPAQTD AATKNMVISC
     GVHGDETAPM ELLDKWIDDI VSGFQPVAER CLFILAHPQA TVRHVRFIEQ NLNRLFDDKP
     HTPSTELAIA DNLKVLLKQF FANTDEHSRW HLDLHCAIRG SKHYSFAVSP KARHPVRSRS
     LMQFIEQAHI EAVMLSNAPS STFSWYSAEH YAAQALTLEL GQVARLGENL LDRLLAFDLA
     MRDLISRHKP EHLPRKSVMY RVSRTIVRLH DDFDFRFSDD VENFTAFMHG EVFGHDGDKP
     LMAKNEGEAI VFPNRKVAIG QRAALMVCKV NTRYEDDQLV YD