ID A0A093SW89_9PASS Unreviewed; 587 AA.
AC A0A093SW89;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Prostaglandin G/H synthase 2 {ECO:0000256|ARBA:ARBA00020406};
DE EC=1.14.99.1 {ECO:0000256|ARBA:ARBA00012440};
DE AltName: Full=Cyclooxygenase-2 {ECO:0000256|ARBA:ARBA00031216};
DE AltName: Full=PHS II {ECO:0000256|ARBA:ARBA00030839};
DE AltName: Full=Prostaglandin H2 synthase 2 {ECO:0000256|ARBA:ARBA00031793};
DE AltName: Full=Prostaglandin-endoperoxide synthase 2 {ECO:0000256|ARBA:ARBA00033144};
DE Flags: Fragment;
GN ORFNames=N305_10959 {ECO:0000313|EMBL:KFW86794.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW86794.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW86794.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW86794.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
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; KL672761; KFW86794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093SW89; -.
DR STRING; 328815.ENSMVIP00005006938; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
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:SF8; PROSTAGLANDIN G_H SYNTHASE 2; 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 Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
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: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:UP000053258}.
FT DOMAIN 6..39
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT ACT_SITE 355
FT /note="For cyclooxygenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT BINDING 358
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"
FT DISULFID 6..16
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW86794.1"
FT NON_TER 587
FT /evidence="ECO:0000313|EMBL:KFW86794.1"
SQ SEQUENCE 587 AA; 67515 MW; 55C6CD6D51C48930 CRC64;
AANPCCSHPC QNRGVCMTTG PDRYQCDCTR TGFYGENCTT PEFFTWLRLT LKPSPNTVHY
ILTHFQGVWN IINNIPFLRD AIMRYVLTSR SHLIDSPPTY NTDYSYKSWE AYSNLSYYTR
SLPPVGLDCP TPMGVKGKKE LPDSKLIVEK FLLRRKFIPD PQGTNVMFTF FAQHFTHQFF
KTDHKKGPGF TTGLGHGVDL NHIYGETLER QLKLRLRKDG KLKYQMIDGE MYPPTVKDTQ
AEMLYPPHVP EHLRFSVGQE VFGLVPGLMM YATIWLREHN RVCDVLRREH PEWDDEQLFQ
TTRLILIGET IKIVIEDYVQ HLSGYHFKLK FDPELLFNQR FQYQNRIAAE FNTLYHWHPL
LPDTFHIHDQ EYTFQQFLYN NSIMLEHGLS HMVKSFSKQS AGRVAGGKNV PAAVQKVAKA
SIDQSRQMRY QSLNEYRKRF MLKPFRSFEE LTGEKEMAAE LEELYGDIDA MELYPGLLVE
KPRPGAIFGE TMVEMGAPFS LKGLMGNAIC SPEYWKPSTF GGKVGFDIIN TASLQKLICN
NVKGCPFTAF HILSPEPTEA TINVSTSKTA MEDINPTLLL KERSAEL
//
