ID J1RGD8_9ACTN Unreviewed; 334 AA.
AC J1RGD8;
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=Phosphotriesterase-family protein {ECO:0000313|EMBL:EJJ03379.1};
GN ORFNames=SU9_29121 {ECO:0000313|EMBL:EJJ03379.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ03379.1};
RN [1] {ECO:0000313|EMBL:EJJ03379.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ03379.1};
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).
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:EJJ03379.1}.
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DR EMBL; AJGV01000184; EJJ03379.1; -; Genomic_DNA.
DR AlphaFoldDB; J1RGD8; -.
DR STRING; 1160718.SU9_29121; -.
DR PATRIC; fig|1160718.3.peg.5891; -.
DR eggNOG; COG1735; Bacteria.
DR HOGENOM; CLU_054760_1_1_11; -.
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:PIRSR601559-51}.
FT REGION 312..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 142
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 142
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 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT MOD_RES 142
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-50,
FT ECO:0000256|PROSITE-ProRule:PRU00679"
SQ SEQUENCE 334 AA; 34130 MW; 3AE16B6B1943C9D3 CRC64;
MVTPATAHGA AVPAVRTVLG DIAPEDLGVC NAHDHLFLRS PRLPGQELDD AGAAAAELGA
FRAAGGAAVI QWTPYGMGRV AAELPGLARE SGVRIVAATG LHQAVHYAPE VLERVRADLA
GLFVAELTVG IGGTGPRAGM IKVAGGFHGL DRHARYTMAA AAEAQRATGA AIGVHLELGT
GALDVLDLLC GELAVPPDRV ILGHLNRAPD LVVHRAAAGA GAYLAFDGPS RAHHATDWRL
PEALAALAGA GFADRILLGG DTTTADARSV NGGPGMPHLL SRHRKRLELA LGADLVTQFL
TANPARAFAA PWARTPHAGQ TSPPGRATDA PATT
//
