ID C4IF05_CLOBU Unreviewed; 391 AA.
AC C4IF05;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Isoaspartyl dipeptidase {ECO:0000256|PIRNR:PIRNR001238};
DE EC=3.4.19.- {ECO:0000256|PIRNR:PIRNR001238};
GN Name=iadA {ECO:0000313|EMBL:EEP55594.1};
GN ORFNames=CLP_3982 {ECO:0000313|EMBL:EEP55594.1};
OS Clostridium butyricum E4 str. BoNT E BL5262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP55594.1, ECO:0000313|Proteomes:UP000003081};
RN [1] {ECO:0000313|EMBL:EEP55594.1, ECO:0000313|Proteomes:UP000003081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.;
RL Submitted (AUG-2009) 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:EEP55594.1}.
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DR EMBL; ACOM01000004; EEP55594.1; -; Genomic_DNA.
DR RefSeq; WP_003410760.1; NZ_ACOM01000004.1.
DR AlphaFoldDB; C4IF05; -.
DR STRING; 1492.ATN24_02665; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_058216_0_0_9; -.
DR Proteomes; UP000003081; 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|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:UP000003081};
KW Zinc {ECO:0000256|PIRNR:PIRNR001238, ECO:0000256|PIRSR:PIRSR001238-3}.
FT DOMAIN 277..377
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 286
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 286
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 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
SQ SEQUENCE 391 AA; 42450 MW; 2E5BA2A6D85E2D79 CRC64;
MISLIKGCRV YSPNDIGIKD VLLAGGKIEG IYDNIELKDD LLKINIIDGN KKLMFPGFID
SHVHIIGGGG EGGYHTRTPE IQLSSLIESG ITSVVGCIGT DGVCRDMNSL IAKVKSLKEE
GMSAYAYTGS YEVPVKTATE SIKSDLMLIE EIIGVGEIAL SDHRSSQPSF DGFVNLVAQS
RVGGLLSNKA GIVNVHLGEG MRRLKYLFDL IEQTEIPAEQ LLPTHINRNS DLFEMGLEYV
KKGGYIDLTT SCDLEHMENG ELRAGEGLGV FLEKGMEIEH MTFSSDGNGS MPRFDKNGNL
AGLGICSVSS LYREVKFAIN EFNVPIDKAI SVITSNVAKL LKLNNKGRIE EGKDADLVIV
DEDNLDIDIV FANGKKVVEK GKAVVKGTFE Q
//
