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Database: UniProt
Entry: A0A0L8I0F9_OCTBM
LinkDB: A0A0L8I0F9_OCTBM
Original site: A0A0L8I0F9_OCTBM 
ID   A0A0L8I0F9_OCTBM        Unreviewed;       612 AA.
AC   A0A0L8I0F9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=prostaglandin-endoperoxide synthase {ECO:0000256|ARBA:ARBA00012440};
DE            EC=1.14.99.1 {ECO:0000256|ARBA:ARBA00012440};
GN   ORFNames=OCBIM_22001586mg {ECO:0000313|EMBL:KOF94520.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF94520.1};
RN   [1] {ECO:0000313|EMBL:KOF94520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF94520.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF94520.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KQ416946; KOF94520.1; -; Genomic_DNA.
DR   RefSeq; XP_014768109.1; XM_014912623.1.
DR   AlphaFoldDB; A0A0L8I0F9; -.
DR   STRING; 37653.A0A0L8I0F9; -.
DR   EnsemblMetazoa; Ocbimv22001586m; Ocbimv22001586m.p; Ocbimv22001586m.g.
DR   EnsemblMetazoa; XM_014912623.1; XP_014768109.1; LOC106867682.
DR   GeneID; 106867682; -.
DR   KEGG; obi:106867682; -.
DR   OMA; NVHYGYK; -.
DR   OrthoDB; 1086441at2759; -.
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:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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:SF38; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 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|PROSITE-ProRule:PRU00076};
KW   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:ARBA00022559};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW   Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..612
FT                   /note="prostaglandin-endoperoxide synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005584057"
FT   DOMAIN          18..56
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          581..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         373
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   612 AA;  70954 MW;  B8E5B34B0B14A489 CRC64;
     MILIYTVSLI MLTALVNAAN PCCSFPCQHK SVCMTKGFDD YICDCSQTGY YGKNCEIPTF
     RQTIISFIKP TPDTVHYILT NFPVLWTIVN NVPFLNNIVM AYVYVSRGQL VDSPPLYVSN
     QTFTYLDIYY NRSTFVRNLP PVPKDCPTPL GVVGPKVLPD TNKLIELFRR QEFKPDPMGT
     SLLFAFMAQH FTHQFFKTDL TKNPDMQWGN QGVDASNIYG KNLHEENLLR TFKDGKMKSQ
     IINNEVWPPH VKDAPVSAKF LDKIDQNFHF AVGHEFFNVV PGLIVFSTVW LREHNRVCNI
     LKKEHPEWLD EQLFQTTKLI IIGEIIKLII EEYVSHLAHY GLNIRFDPEL LFNQRYQYQN
     RIAIEFNHLY HWHPFIPDIF NINGTMYTNR EFYYHPEIVV KHGMKAFVDS LSRQTAGQMT
     AYNHGAVTLH VAKEIIEHGR LLRLQSFNNY RRRFNLKPYK NFFELTGNME LANILENFYG
     DVEAVEMYVG MIAEKRQHKS LFGQTIIEMG APFSVKGLMS NPICSPGWWK PSTFGGDVGF
     NIVKTQTFKK LFCQNMKDGC GLVSLRIPEW TEEYEESRRK IENEAMYRMP STKESTSEKP
     LMSNSKPQSN EL
//
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