ID K6ZXJ3_9ALTE Unreviewed; 382 AA.
AC K6ZXJ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, 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 Name=iadA {ECO:0000313|EMBL:GAC28040.1};
GN ORFNames=GPAL_1162 {ECO:0000313|EMBL:GAC28040.1};
OS Glaciecola pallidula DSM 14239 = ACAM 615.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121922 {ECO:0000313|EMBL:GAC28040.1, ECO:0000313|Proteomes:UP000006251};
RN [1] {ECO:0000313|EMBL:GAC28040.1, ECO:0000313|Proteomes:UP000006251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 615 {ECO:0000313|EMBL:GAC28040.1,
RC ECO:0000313|Proteomes:UP000006251};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(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: 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:GAC28040.1}.
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DR EMBL; BAEQ01000018; GAC28040.1; -; Genomic_DNA.
DR RefSeq; WP_006009907.1; NZ_KE386814.1.
DR AlphaFoldDB; K6ZXJ3; -.
DR STRING; 1121922.GCA_000428905_00004; -.
DR OrthoDB; 9776455at2; -.
DR Proteomes; UP000006251; 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, ECO:0000313|EMBL:GAC28040.1};
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|PIRNR:PIRNR001238, ECO:0000256|PIRSR:PIRSR001238-3}.
FT DOMAIN 51..368
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-1"
FT BINDING 60
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 62
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 194
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 223
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 280
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"
SQ SEQUENCE 382 AA; 41941 MW; 26882AD8F46338F8 CRC64;
MITIIKNADV YAPENLGLKH ILIAENKIVY VGDILPELNL EHNIVDAEGC IVMPGFIDGH
THITGGGGEA GFSTRVPAVP LSKFTRAGVT TAVGLLGTDD LTRSTESLVA QVYALREEGF
SAYCYTGGYH LPATTLTGSV KSDIVFIEPI IGVGELAISD HRSSQPTLNE LLKVASEAHV
ARLMTGKAGM LHLHLGDGER GLSLVREALD SAEIPPRTYN PTHINRQRFL FEEACDLAKR
GCWVDVTAFE TGDVGFEPGE ALLRYMQQDL PQDKLTISSD GGGCLPDFHS DGSLKKMDFA
ESQSMTDIFY KLVDDDQAVE KFLPFFTKNV ATLMNFHHKG RIKEGADADI IILNKQNRIE
HVMAMGHWHV KYKQQVKKGT FE
//
