ID A0A0F2JEL4_9FIRM Unreviewed; 389 AA.
AC A0A0F2JEL4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Isoaspartyl dipeptidase {ECO:0000256|PIRNR:PIRNR001238};
DE EC=3.4.19.- {ECO:0000256|PIRNR:PIRNR001238};
GN ORFNames=UF75_2265 {ECO:0000313|EMBL:KJR47352.1};
OS Desulfosporosinus sp. I2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR47352.1, ECO:0000313|Proteomes:UP000033442};
RN [1] {ECO:0000313|EMBL:KJR47352.1, ECO:0000313|Proteomes:UP000033442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I2 {ECO:0000313|EMBL:KJR47352.1,
RC ECO:0000313|Proteomes:UP000033442};
RA Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., Ravin N.V.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJR47352.1}.
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DR EMBL; JYNH01000036; KJR47352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2JEL4; -.
DR PATRIC; fig|1617025.3.peg.2360; -.
DR Proteomes; UP000033442; 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:SF97; AMIDOHYDROLASE-RELATED DOMAIN-CONTAINING PROTEIN; 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|ARBA:ARBA00022801, 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 Reference proteome {ECO:0000313|Proteomes:UP000033442};
KW Zinc {ECO:0000256|PIRNR:PIRNR001238, ECO:0000256|PIRSR:PIRSR001238-3}.
FT DOMAIN 53..371
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-1"
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 64
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 69..71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 196
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 225
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 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 283
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 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
SQ SEQUENCE 389 AA; 42326 MW; B09A8E08AF6C2F13 CRC64;
MVWKLIKNAK LYCPECSENT DILVVGTSIA AIGKNIGLPN FVEGEEIDLQ DKTVVPGFID
AHVHICGGGG EAGPASRTPE INLSQLTRAG TTTVVGCLGT DSISRSMSEL LVKANALQDE
GISTFIYSGG YQVPMRTLLV TLEQDLVLIH KVIGAGEIAI SDHRSGQPQI AQLEHLAAQA
RVGGMLAGKA GVVHLHLGEG KRGLDPIFKI LEETEIPITQ FMPTHINRTH ALLEQGIKFL
LAGGYIDLTA GCDDFPEELQ VPSVLKMLYQ RQILNDRITV TSDGNGSMPQ YNETGVLIGM
GIGSVEVLWR DIRKSVVHYG LPLEVALRTI TSNVANVLRL KNKGIIRVGY DADLVVLDQD
LEVQDVWAMG KCMLRNRKTQ VWGTYEPRN
//
