ID   A0A087D767_9BIFI        Unreviewed;       329 AA.
AC   A0A087D767;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Phosphotriesterase family protein {ECO:0000313|EMBL:KFI91367.1};
DE            EC=3.1.8.1 {ECO:0000313|EMBL:KFI91367.1};
GN   ORFNames=BSCA_2056 {ECO:0000313|EMBL:KFI91367.1};
OS   Bifidobacterium scardovii.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI91367.1, ECO:0000313|Proteomes:UP000029033};
RN   [1] {ECO:0000313|EMBL:KFI91367.1, ECO:0000313|Proteomes:UP000029033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI91367.1,
RC   ECO:0000313|Proteomes:UP000029033};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601559-51};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR601559-51};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000256|PROSITE-ProRule:PRU00679}.
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:KFI91367.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JGZO01000023; KFI91367.1; -; Genomic_DNA.
DR   RefSeq; WP_033518195.1; NZ_JGZO01000023.1.
DR   AlphaFoldDB; A0A087D767; -.
DR   STRING; 158787.BSCA_2056; -.
DR   GeneID; 85165334; -.
DR   eggNOG; COG1735; Bacteria.
DR   OrthoDB; 9795018at2; -.
DR   Proteomes; UP000029033; Unassembled WGS sequence.
DR   GO; GO:0004063; F:aryldialkylphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001559; Phosphotriesterase.
DR   PANTHER; PTHR10819; PHOSPHOTRIESTERASE-RELATED; 1.
DR   PANTHER; PTHR10819:SF3; PHOSPHOTRIESTERASE-RELATED PROTEIN; 1.
DR   Pfam; PF02126; PTE; 1.
DR   PIRSF; PIRSF016839; PhP; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KFI91367.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601559-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029033}.
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT   MOD_RES         156
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601559-50,
FT                   ECO:0000256|PROSITE-ProRule:PRU00679"
SQ   SEQUENCE   329 AA;  36336 MW;  EE0189E1AAF16F50 CRC64;
     MAFARTIFGD VDPSTLGVVD CHDHLIRVGA GEVYIDGDHQ LDSVEKAIEE GGYFAEASRK
     WSPNGGTVVD MCPINCGRDL DKLAEVTKAV DGLQVIAATG FHREHVYLET QSHWINRYGV
     DKVAELVIAD IREGIDRNDY SGPIVDRTPY KAGVIKVGTA YGKITKFECK CMEAAAIAAI
     ETGCPINTHT TYGTCGLEQA EGFLELGVPA NQIAIGHIQR NADVYYLEQI LKLGVYLEID
     GTNRIKYQPD SNRMMELKAF YEDGFADRIL LGTDSGKRGY QKAYGATSGV DYNPAVDGPR
     MVDEGFDREY IDKLLMKNAQ EFFTFKKEG
//