ID I3JX72_ORENI Unreviewed; 597 AA.
AC I3JX72;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Prostaglandin G/H synthase 1 {ECO:0000256|ARBA:ARBA00020404};
DE EC=1.14.99.1 {ECO:0000256|ARBA:ARBA00012440};
DE AltName: Full=Cyclooxygenase-1 {ECO:0000256|ARBA:ARBA00031217};
DE AltName: Full=Prostaglandin H2 synthase 1 {ECO:0000256|ARBA:ARBA00031794};
DE AltName: Full=Prostaglandin-endoperoxide synthase 1 {ECO:0000256|ARBA:ARBA00033143};
GN Name=LOC100699955 {ECO:0000313|Ensembl:ENSONIP00000013467.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000013467.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000013467.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-
CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:136655;
CC Evidence={ECO:0000256|ARBA:ARBA00036409};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456;
CC Evidence={ECO:0000256|ARBA:ARBA00036409};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-
CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:90850;
CC Evidence={ECO:0000256|ARBA:ARBA00036358};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452;
CC Evidence={ECO:0000256|ARBA:ARBA00036358};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-
CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:77895;
CC Evidence={ECO:0000256|ARBA:ARBA00036313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448;
CC Evidence={ECO:0000256|ARBA:ARBA00036313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-
CC octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:77852;
CC Evidence={ECO:0000256|ARBA:ARBA00035976};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460;
CC Evidence={ECO:0000256|ARBA:ARBA00035976};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004702}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC {ECO:0000256|ARBA:ARBA00008928}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_003454212.1; XM_003454164.4.
DR AlphaFoldDB; I3JX72; -.
DR GlyCosmos; I3JX72; 3 sites, No reported glycans.
DR Ensembl; ENSONIT00000013477.2; ENSONIP00000013467.1; ENSONIG00000010712.2.
DR GeneID; 100699955; -.
DR KEGG; onl:100699955; -.
DR CTD; 5742; -.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00390000010743; -.
DR OrthoDB; 1086441at2759; -.
DR TreeFam; TF329675; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000005207; Linkage group LG12.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09816; prostaglandin_endoperoxide_synthase; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR PANTHER; PTHR11903:SF6; PROSTAGLANDIN G_H SYNTHASE 1; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..597
FT /note="Prostaglandin G/H synthase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003673584"
FT DOMAIN 31..69
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT ACT_SITE 384
FT /note="For cyclooxygenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT BINDING 387
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 597 AA; 68746 MW; 30CA3115624E2F04 CRC64;
MKAFSIFIWV FITLLLLLLL ESSSCAGDSS VVNPCCYYPC QHAGVCMRFG TDSFKCDCTR
TGFYGDNCTI PEFWTRIQLM LKPSPSVTHF ILTHFPWFWY LINNSFLRDT FMRLVLTARS
DLIPSPPTYN TKYGYINWES YSNITYYTRL LPPIPEDCPL PMGAKGKPVL PDAKVFVERF
FKRQKFRPDP QGTNLMFTFM AQHFTHQFFK TNHKVQGGFT KGLGHGVDAS NIYGEDLVRQ
HQLRLHKDGK LKYQLVNGEV YPPTVSEVPV HMVYPENIPA DKRLAIGQEV FGILPGLTTY
ATIWLREHNR VCDILKAEHP TWDDEQLFQT ARLILIGEII NIIIEEYVQH LSGYMLDLKF
DPSLLFNTRF QYNNRIALEF CHLYHWHPLM PDSIVIEGEE IPYSQFLYNT SLLMHYGVER
LVDAFSRQIA GQIGGGHNSH QVVLKVAEMV IRESRATRVQ PFNEYRKRFN LKPYTSFDEL
TDNTEIARGL EEVYGDIDAL EFYPGIMLEK SRPNAIFGES MVEMGAPFSL KGLLGNPICS
PEYWKPSTFG GETGFNIVKT ATLKKLVCLN SKWCPYVDFH VPRNEDEAKP RKPSTEL
//
