ID C3ZWS9_BRAFL Unreviewed; 710 AA.
AC C3ZWS9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=prostaglandin-endoperoxide synthase {ECO:0000256|ARBA:ARBA00012440};
DE EC=1.14.99.1 {ECO:0000256|ARBA:ARBA00012440};
GN Name=LOC118421716 {ECO:0000313|RefSeq:XP_035685091.1};
GN ORFNames=BRAFLDRAFT_129952 {ECO:0000313|EMBL:EEN42998.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN42998.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN42998.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN42998.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
RN [2] {ECO:0000313|RefSeq:XP_035685091.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035685091.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035685091.1};
RG RefSeq;
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 EMBL; GG666703; EEN42998.1; -; Genomic_DNA.
DR RefSeq; XP_002586987.1; XM_002586941.1.
DR RefSeq; XP_035685091.1; XM_035829198.1.
DR STRING; 7739.C3ZWS9; -.
DR KEGG; bfo:118421716; -.
DR eggNOG; KOG2408; Eukaryota.
DR InParanoid; C3ZWS9; -.
DR OMA; TIKHERN; -.
DR OrthoDB; 1086441at2759; -.
DR Proteomes; UP000001554; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IBA:GO_Central.
DR GO; GO:0019371; P:cyclooxygenase pathway; IBA:GO_Central.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..710
FT /note="prostaglandin-endoperoxide synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041196742"
FT DOMAIN 19..56
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 574..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT ACT_SITE 371
FT /note="For cyclooxygenase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-1"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT BINDING 374
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 710 AA; 80066 MW; 7441FAF95BDA57A1 CRC64;
MNGAIIAICL TLLPVLIAAE NPCCSMPCQN MGVCMREGDS YSCDCTRTGY YGQNCDIPEF
WTSIKVALKP SKKTTHHLLT NYKWLWNIVN RIPFLSKFIM RAVYKIRSAT VDSPPMYHTG
HDYTSWDTYA DRSYYTRALP PVPPGCPTPM GTAGRKELPS PQYIAETFLA RRRFIPDKRR
TNVLFNFMAQ HFTHQFFKTD FKKGAGRTWG DHGVDLSHIY GETVERQHQL RSFTDGKLKF
QRVEGEVYPP SLADAPVHMI YPPYVPEGKR FAIGHEFFGL LPGLFVYSTV WLREHNRVCD
VMKELHPDWD DERLFQTARL ILTGETINII INEYVQHLSG YNFDLFWDPE LLFSDQFQYQ
NRIFVEFNHL YHWHPLMPDQ FHINGSTYGM KDYLFNTDLV FKHGFGTTVD AMSRQIAGQI
GPKNIGPVNL KVAVETIKHE RNLRMQGLNQ YRKRFGIPPY KTFLELTGGD AEMADQLEEA
YGDVDAVELY VGLMVEQPAP GSVTSETIIE MGGPFSVKGL LSNPLCSPQW WKPSTFGGEA
GFRMVKTATL KDLFCRNTAG PCGLVSFAVP EDVQPTGLPE EQDASSQGKG ASQNDADLVP
VNGVLSSQDK HLHKEEKTSQ DGSQDPETSS KVTANEKPVA KNEKLPKNGV AQKKEFQNGS
PKNGRASKND VPKNEPAPKN GLPTAFPKNG AAPRTYVNRT SCKQCDRIEL
//
