ID G3HT86_CRIGR Unreviewed; 479 AA.
AC G3HT86;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
GN ORFNames=I79_014108 {ECO:0000313|EMBL:EGW06948.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW06948.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000368,
CC ECO:0000256|RuleBase:RU368025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
CC + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81;
CC Evidence={ECO:0000256|ARBA:ARBA00000450};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR602640-2,
CC ECO:0000256|RuleBase:RU368025};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC 2, ECO:0000256|RuleBase:RU368025};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- PTM: Glycosylated. {ECO:0000256|PIRSR:PIRSR602640-4}.
CC -!- SIMILARITY: Belongs to the paraoxonase family.
CC {ECO:0000256|ARBA:ARBA00008595, ECO:0000256|RuleBase:RU368025}.
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DR EMBL; JH000690; EGW06948.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HT86; -.
DR STRING; 10029.G3HT86; -.
DR eggNOG; ENOG502QUCT; Eukaryota.
DR InParanoid; G3HT86; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR008364; Paraoxonase2.
DR PANTHER; PTHR11799; PARAOXONASE; 1.
DR PANTHER; PTHR11799:SF17; SERUM PARAOXONASE_ARYLESTERASE 2; 1.
DR Pfam; PF01731; Arylesterase; 2.
DR PRINTS; PR01785; PARAOXONASE.
DR PRINTS; PR01787; PARAOXONASE2.
DR SUPFAM; SSF75011; 3-carboxy-cis,cis-mucoante lactonizing enzyme; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR602640-2, ECO:0000256|RuleBase:RU368025};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR602640-3,
KW ECO:0000256|RuleBase:RU368025};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR602640-
KW 4};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368025};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2,
KW ECO:0000256|RuleBase:RU368025};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT DISULFID 42..477
FT /note="In form B"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-3"
SQ SEQUENCE 479 AA; 53779 MW; F8CB03B05050ED27 CRC64;
MGRLVALSLL GIGLALLGER FLALRNRLKA SREVESVDLP NCHLIKGIEA GAEDIDVLPN
GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KEEKPRALEL RVSWGFDLAS FNPHGISTFI
DGDDTVYLFV VNHPEFKNTV EIFKFEEEEN SLLHLKTIKH ELLPSVNDIV AVGPAHFYAT
NDHYFSDPFL KYLETYLNLR WANVVYYSPD EVKLVAEGFD SANGINISPD KKYVYVADIL
AHEIHVLEKQ PNMNLTQLKG LKYPGMPNFA PDKPGRIFLM DLNEQNPKAQ ALEISDGFDK
ESLNPHGIST FIDKDNTVYL YVVNHPHMGS TVEIFKFEEQ QRSLVHLKTI KHELLKRYVY
VADVTAKNIH IMEKHDNWDL TQVKVIHLGT LVDNLTIDPA TGDILAGCHP NPMKLLNYNP
EDPPGSEVLR IQDVLSDKPR VNTLYANNGS VLQASTVASV YHGIMLIGTV FHKALYCEL
//
