ASTE_VIBVU
ID ASTE_VIBVU Reviewed; 342 AA.
AC Q8D926;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
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}; OrderedLocusNames=VV1_2783;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AE016795; AAO11125.2; -; Genomic_DNA.
DR RefSeq; WP_011080619.1; NC_004459.3.
DR AlphaFoldDB; Q8D926; -.
DR SMR; Q8D926; -.
DR EnsemblBacteria; AAO11125; AAO11125; VV1_2783.
DR KEGG; vvu:VV1_2783; -.
DR HOGENOM; CLU_071608_0_0_6; -.
DR OMA; FIIAHPE; -.
DR UniPathway; UPA00185; UER00283.
DR Proteomes; UP000002275; Chromosome 1.
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_0000174652"
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; 38889 MW; 604C50F4436FCDE4 CRC64;
MTNSLFRQSF LSDTLNMQQS VEAKATTLSN GVRLQLHQRG VLEVIPANNS AETKNIILSS
GIHGDETAPM ELIDKIVHDI ETGFQDVQAR CLFIIAHPEA TNAHTRFIEE NLNRLFDEKE
HQPSKELVIA DQLKLLVKAF FDNTPVESRW HLDLHCAIRA SKHYSFAISP KTRHPTRSKA
LVDFVNHSHV EALLLSNSPS STFSWFSAEY YSAQALTMEL GRVARIGENE LERFTALDLT
MRDLIAEVTP EHLPKPAITY RVSRTIVRLH QDFDFRFDDQ VENFTSFMHG EVFGHDGDKP
LMAKNDNEAI VFPNRNVAIG QRAALMVCEV KARFEDDQLV YD