ID V7ISH6_SALET Unreviewed; 390 AA.
AC V7ISH6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Isoaspartyl dipeptidase {ECO:0000256|PIRNR:PIRNR001238};
DE EC=3.4.19.- {ECO:0000256|PIRNR:PIRNR001238};
GN ORFNames=A628_00843 {ECO:0000313|EMBL:ETA89120.1};
OS Salmonella enterica subsp. enterica serovar Cubana str. 76814.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192560 {ECO:0000313|EMBL:ETA89120.1, ECO:0000313|Proteomes:UP000018534};
RN [1] {ECO:0000313|EMBL:ETA89120.1, ECO:0000313|Proteomes:UP000018534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=76814 {ECO:0000313|EMBL:ETA89120.1};
RX PubMed=24459266;
RA Benahmed F.H., Gopinath G.R., Wang H., Jean-Gilles Beaubrun J., Grim C.,
RA Cheng C.M., McClelland M., Ayers S., Abbott J., Desai P., Frye J.G.,
RA Weinstock G., Hammack T.S., Hanes D.E., Rasmussen M.A., Davidson M.K.;
RT "Whole-Genome Sequencing of Salmonella enterica subsp. enterica Serovar
RT Cubana Strains Isolated from Agricultural Sources.";
RL Genome Announc. 2:e01184-13(2014).
CC -!- FUNCTION: Catalyzes the hydrolytic cleavage of a subset of L-
CC isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins
CC damaged by L-isoaspartyl residues formation.
CC {ECO:0000256|PIRNR:PIRNR001238}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR001238,
CC ECO:0000256|PIRSR:PIRSR001238-3};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRNR:PIRNR001238,
CC ECO:0000256|PIRSR:PIRSR001238-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001238}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000256|PIRSR:PIRSR001238-50}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000256|PIRNR:PIRNR001238}.
CC -!- SIMILARITY: Belongs to the peptidase M38 family.
CC {ECO:0000256|PIRNR:PIRNR001238}.
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:ETA89120.1}.
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DR EMBL; AZGR01000016; ETA89120.1; -; Genomic_DNA.
DR RefSeq; WP_020898333.1; NZ_KI635586.1.
DR AlphaFoldDB; V7ISH6; -.
DR PATRIC; fig|1192560.4.peg.773; -.
DR HOGENOM; CLU_058216_0_0_6; -.
DR Proteomes; UP000018534; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR010229; Pept_M38_dipep.
DR NCBIfam; TIGR01975; isoAsp_dipep; 1.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001238; IadA; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001238};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR001238,
KW ECO:0000256|PIRSR:PIRSR001238-3};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR001238};
KW Protease {ECO:0000256|PIRNR:PIRNR001238};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR001238}.
FT DOMAIN 265..373
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-1"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-3"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT MOD_RES 162
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-50"
SQ SEQUENCE 390 AA; 40427 MW; 9FDB3579BE842462 CRC64;
MPDLSAAEFT LLQGAHLFAP EDRGICDVLL ANGKIIAVGA DIPGDIVPDC TVINLSGRML
CPGFIDQHVH LIGGGGEAGP TTRTPEVSLS RLTEAGITTV VGLLGTDSVS RHPASLLAKT
RALNEEGITA WMLTGAYHVP SPTITGSVEK DVALIDRVIG VKCAVSDHRS AAPSGNQLAS
MAAESRVGGL LGGKPGVSVF HMGSSKKGLQ PLYDILENSD VPIGKLLPTH VNRSESLFEQ
ALAFALKGGV IDITTSIPDP VAPAEGIARA IKAGVPLSRV TLSSDGNGSQ PLFDAAGNLT
GIGVAGFESL LETLQTLVNH YGFSLTDALR PLTTSVAAFL SLDGKGEIRP GNDADLLVFS
ADLRIEQVYA RGKRMVNEGK ACVKGTFEPA
//
