PHP_SACS2
ID PHP_SACS2 Reviewed; 314 AA.
AC Q97VT7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Aryldialkylphosphatase;
DE EC=3.1.8.1;
DE AltName: Full=Paraoxonase;
DE Short=SsoPox;
DE AltName: Full=Phosphotriesterase-like lactonase;
GN Name=php; OrderedLocusNames=SSO2522;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=15909078; DOI=10.1007/s00792-005-0445-4;
RA Merone L., Mandrich L., Rossi M., Manco G.;
RT "A thermostable phosphotriesterase from the archaeon Sulfolobus
RT solfataricus: cloning, overexpression and properties.";
RL Extremophiles 9:297-305(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), COFACTOR, METAL-BINDING SITES,
RP SUBUNIT, AND CARBOXYLATION AT LYS-137.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=18486146; DOI=10.1016/j.jmb.2008.04.022;
RA Elias M., Dupuy J., Merone L., Mandrich L., Porzio E., Moniot S., Rochu D.,
RA Lecomte C., Rossi M., Masson P., Manco G., Chabriere E.;
RT "Structural basis for natural lactonase and promiscuous phosphotriesterase
RT activities.";
RL J. Mol. Biol. 379:1017-1028(2008).
CC -!- FUNCTION: Has a low paraoxonase activity. Also active, but with a lower
CC activity, against other organo-phosphorus insecticides such as Dursban,
CC Coumaphos, pNP-butanoate or parathion. {ECO:0000269|PubMed:15909078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl
CC alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:15909078};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18486146};
CC Note=Binds 1 Co(2+) ion per subunit. {ECO:0000269|PubMed:18486146};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:18486146};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:18486146};
CC -!- ACTIVITY REGULATION: Inactivated by EDTA and o-phenanthroline.
CC {ECO:0000269|PubMed:15909078}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for paraoxon (at pH 8.0) {ECO:0000269|PubMed:15909078};
CC KM=0.205 mM for methyl-paraoxon (at pH 8.0)
CC {ECO:0000269|PubMed:15909078};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:15909078};
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:15909078};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18486146}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; AE006641; AAK42653.1; -; Genomic_DNA.
DR EMBL; AY775568; AAW47234.1; -; Genomic_DNA.
DR PIR; F90424; F90424.
DR RefSeq; WP_009988477.1; NC_002754.1.
DR PDB; 2VC5; X-ray; 2.60 A; A/B/C/D=1-314.
DR PDB; 2VC7; X-ray; 2.05 A; A/B/C/D=1-314.
DR PDB; 3UF9; X-ray; 2.68 A; A/B/C/D=1-314.
DR PDB; 4KER; X-ray; 2.60 A; A/B/C/D=1-314.
DR PDB; 4KES; X-ray; 2.10 A; A/B/C/D=1-314.
DR PDB; 4KET; X-ray; 2.00 A; A/B/C/D=1-314.
DR PDB; 4KEU; X-ray; 2.20 A; A/B/C/D=1-314.
DR PDB; 4KEV; X-ray; 2.65 A; A/B/C/D=1-314.
DR PDB; 4KEZ; X-ray; 1.85 A; A/B/C/D=1-314.
DR PDB; 4KF1; X-ray; 2.00 A; A/B/C/D=1-314.
DR PDB; 5VRI; X-ray; 2.15 A; A/B/C/D=1-314.
DR PDB; 5VRK; X-ray; 1.40 A; A/B=1-314.
DR PDB; 5VSA; X-ray; 2.00 A; A/B/C/D=1-314.
DR PDB; 5W3U; X-ray; 2.50 A; A/B/C/D=1-314.
DR PDB; 5W3W; X-ray; 2.95 A; A/B/C/D=1-314.
DR PDB; 5W3Z; X-ray; 2.55 A; A/B/C/D=1-314.
DR PDBsum; 2VC5; -.
DR PDBsum; 2VC7; -.
DR PDBsum; 3UF9; -.
DR PDBsum; 4KER; -.
DR PDBsum; 4KES; -.
DR PDBsum; 4KET; -.
DR PDBsum; 4KEU; -.
DR PDBsum; 4KEV; -.
DR PDBsum; 4KEZ; -.
DR PDBsum; 4KF1; -.
DR PDBsum; 5VRI; -.
DR PDBsum; 5VRK; -.
DR PDBsum; 5VSA; -.
DR PDBsum; 5W3U; -.
DR PDBsum; 5W3W; -.
DR PDBsum; 5W3Z; -.
DR AlphaFoldDB; Q97VT7; -.
DR SMR; Q97VT7; -.
DR STRING; 273057.SSO2522; -.
DR EnsemblBacteria; AAK42653; AAK42653; SSO2522.
DR GeneID; 44128246; -.
DR KEGG; sso:SSO2522; -.
DR PATRIC; fig|273057.12.peg.2599; -.
DR eggNOG; arCOG07263; Archaea.
DR HOGENOM; CLU_054760_1_0_2; -.
DR InParanoid; Q97VT7; -.
DR OMA; MVKCGFI; -.
DR PhylomeDB; Q97VT7; -.
DR BRENDA; 3.1.1.25; 6163.
DR BRENDA; 3.1.1.81; 6163.
DR BRENDA; 3.1.8.1; 6163.
DR EvolutionaryTrace; Q97VT7; -.
DR PRO; PR:Q97VT7; -.
DR Proteomes; UP000001974; Chromosome.
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 CDD; cd00530; PTE; 1.
DR InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR PIRSF; PIRSF016839; PhP; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Direct protein sequencing; Hydrolase; Iron;
KW Metal-binding; Reference proteome.
FT CHAIN 1..314
FT /note="Aryldialkylphosphatase"
FT /id="PRO_0000388684"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT BINDING 24
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT BINDING 137
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT BINDING 170
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT BINDING 199
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT BINDING 256
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:18486146,
FT ECO:0007744|PDB:2VC5, ECO:0007744|PDB:2VC7,
FT ECO:0007744|PDB:3UF9, ECO:0007744|PDB:4KER,
FT ECO:0007744|PDB:4KES, ECO:0007744|PDB:4KET,
FT ECO:0007744|PDB:4KEU, ECO:0007744|PDB:4KEV,
FT ECO:0007744|PDB:4KEZ, ECO:0007744|PDB:4KF1"
FT MOD_RES 137
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679,
FT ECO:0000269|PubMed:18486146, ECO:0007744|PDB:2VC5,
FT ECO:0007744|PDB:2VC7, ECO:0007744|PDB:3UF9,
FT ECO:0007744|PDB:4KER, ECO:0007744|PDB:4KES,
FT ECO:0007744|PDB:4KET, ECO:0007744|PDB:4KEU,
FT ECO:0007744|PDB:4KEV, ECO:0007744|PDB:4KEZ,
FT ECO:0007744|PDB:4KF1"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:5VRK"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2VC7"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5VRK"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:5VRK"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5VRK"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:4KEZ"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4KEZ"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:4KEZ"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 298..305
FT /evidence="ECO:0007829|PDB:5VRK"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:5VRK"
SQ SEQUENCE 314 AA; 35565 MW; B5A28F80C3CB1A31 CRC64;
MRIPLVGKDS IESKDIGFTL IHEHLRVFSE AVRQQWPHLY NEDEEFRNAV NEVKRAMQFG
VKTIVDPTVM GLGRDIRFME KVVKATGINL VAGTGIYIYI DLPFYFLNRS IDEIADLFIH
DIKEGIQGTL NKAGFVKIAA DEPGITKDVE KVIRAAAIAN KETKVPIITH SNAHNNTGLE
QQRILTEEGV DPGKILIGHL GDTDNIDYIK KIADKGSFIG LDRYGLDLFL PVDKRNETTL
RLIKDGYSDK IMISHDYCCT IDWGTAKPEY KPKLAPRWSI TLIFEDTIPF LKRNGVNEEV
IATIFKENPK KFFS
