ID F9VLV9_ARTSS Unreviewed; 397 AA.
AC F9VLV9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Isoaspartyl dipeptidase {ECO:0000256|PIRNR:PIRNR001238};
DE EC=3.4.19.- {ECO:0000256|PIRNR:PIRNR001238};
GN OrderedLocusNames=SFBM_1358 {ECO:0000313|EMBL:BAK57117.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK57117.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK57117.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
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}.
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DR EMBL; AP012202; BAK57117.1; -; Genomic_DNA.
DR RefSeq; WP_005805203.1; NC_015913.1.
DR AlphaFoldDB; F9VLV9; -.
DR STRING; 1029718.SFBM_1358; -.
DR KEGG; asf:SFBM_1358; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_058216_0_0_9; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000001636; Chromosome.
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 Zinc {ECO:0000256|PIRNR:PIRNR001238, ECO:0000256|PIRSR:PIRSR001238-3}.
FT DOMAIN 58..380
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-1"
FT BINDING 67
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
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 74..76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
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 291
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 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001238-2"
SQ SEQUENCE 397 AA; 43703 MW; 4DFF3766BAE0B07E CRC64;
MGAILIVTIV KNVEIYSPDN IGKKDVVILF NKIEGIYDEF KYGNCFTEYE IIDGTGLIMF
PGLIDSHVHI SGGGGESGFK SRTPEINFFD LISGGITTVV GCLGTDSICR NMNNLLAKAY
GLEEEGISSY IYTGSYEIPV KTITNSIKSD LMLIPKVIGV GEIALSDYRS SKPSFEEFIK
VIYDARVGGL LANKKGIVHI HIGDSEDGLK YLFELCMNKD ISLDQIIPTH VNRNKKLLNS
AIEYGIKGGY FDLTSSYVRG IKEEEELRVS NILPNIISDG VAISHITCSS DAQGSLPIIG
DDGKFAGIGI GKPKSLYNEI KELLISNSLP KSDIISIVTK NVANILGLHY KGEIKRYNDA
DFILVDNKDY ELKYVFSNGK KMMEEGKILA KETFIKE
//
