ID V9XL46_9NOCA Unreviewed; 323 AA.
AC V9XL46;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Phosphotriesterase {ECO:0000313|EMBL:AHD22700.1};
GN ORFNames=Y013_19735 {ECO:0000313|EMBL:AHD22700.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22700.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD22700.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD22700.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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}.
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DR EMBL; CP006996; AHD22700.1; -; Genomic_DNA.
DR RefSeq; WP_006551850.1; NC_023150.1.
DR AlphaFoldDB; V9XL46; -.
DR GeneID; 29940134; -.
DR KEGG; rpy:Y013_19735; -.
DR PATRIC; fig|1435356.3.peg.3978; -.
DR eggNOG; COG1735; Bacteria.
DR HOGENOM; CLU_054760_1_0_11; -.
DR Proteomes; UP000018781; 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 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 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 147
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 147
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 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT MOD_RES 147
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-50,
FT ECO:0000256|PROSITE-ProRule:PRU00679"
SQ SEQUENCE 323 AA; 35678 MW; E7E0586807478415 CRC64;
MTSVDTVRGP LDTGRLGRVL MHEHVFVLGE EIRTNFPDYP SPWDEDERVD DAVAKLKALS
ERGIDTIVDP TVVGLGRYIP RIQRVAERVD ISIVVATGLY TYNDLPFQFH NVGPGLLVDG
PEPLTELFVK DIREGIAGTG VRAGMLKCAI EIPGLTPGVE RVMRAVGQAH VETGVPITVH
TNPHTGSGQV AQRVLAEEGV DLTKVVIGHS GDSTDLDYLR RIADAGSILG MDRFGLDLLL
PFEQRVDTVV ALVEAGYTER MVLSHDASCF IDWFPHDVKQ TAVPNWNYNH ISDEVLPALR
ERGVTDEQIT TMLVDNPRRI FER
//
