ID J2A1B2_9ACTN Unreviewed; 331 AA.
AC J2A1B2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Aryldialkylphosphatase {ECO:0000313|EMBL:EJJ07906.1};
DE SubName: Full=Phosphotriesterase {ECO:0000313|EMBL:QTZ94342.1};
GN ORFNames=SU9_025240 {ECO:0000313|EMBL:QTZ94342.1}, SU9_06345
GN {ECO:0000313|EMBL:EJJ07906.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ07906.1};
RN [1] {ECO:0000313|EMBL:EJJ07906.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ07906.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ94342.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ94342.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR601559-52};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR601559-52};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000256|PROSITE-ProRule:PRU00679}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00679}.
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DR EMBL; AJGV01000050; EJJ07906.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ94342.1; -; Genomic_DNA.
DR RefSeq; WP_006602845.1; NZ_CP072931.1.
DR AlphaFoldDB; J2A1B2; -.
DR STRING; 1160718.SU9_06345; -.
DR KEGG; sauh:SU9_025240; -.
DR PATRIC; fig|1160718.3.peg.1292; -.
DR eggNOG; COG1735; Bacteria.
DR HOGENOM; CLU_054760_1_1_11; -.
DR OrthoDB; 9795018at2; -.
DR Proteomes; UP000009036; Chromosome.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR601559-52};
KW Reference proteome {ECO:0000313|Proteomes:UP000009036}.
FT REGION 299..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 200
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 257
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
SQ SEQUENCE 331 AA; 34651 MW; 0D7130163F4AE61B CRC64;
MNELLQTVAG PLPVSAVRGP VLAHEHLALD LTRGADRAAT LTPGHRAAIT EELAALRREF
GLSLVIELTC RGMGRDVAGM ARIAADASVA VVAATGWYYE PFHPEELSRT SAERLARTLV
GEIERGCGGS GIRPGVIGEV GSHGDLPSEP EARTLRAAAL AATATGLSVA THAQFGRGGL
AQLELLTAAG LPPHRVSIGH QDLLDDPAVH RELAASGAYI AFDTVGKESY QSDRVRLRLL
LALLASGFAD RALLSCDVSR HGYLVSEGGM GYGHLFRSFL PRLRAAGVDE ETIDGVTRRN
PLRFLTGRDG PAPAAGGRPA DGPAQPAGPP R
//
