ID A0A1B8C0D0_9PEZI Unreviewed; 1063 AA.
AC A0A1B8C0D0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Prostaglandin-endoperoxide synthase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=VE00_09647 {ECO:0000313|EMBL:OBT40301.1};
OS Pseudogymnoascus sp. WSF 3629.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT40301.1, ECO:0000313|Proteomes:UP000091997};
RN [1] {ECO:0000313|EMBL:OBT40301.1, ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT40301.1,
RC ECO:0000313|Proteomes:UP000091997};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR EMBL; KV454693; OBT40301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8C0D0; -.
DR STRING; 1622147.A0A1B8C0D0; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000091997; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000091997}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 367
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 1063 AA; 118594 MW; 06C1D717757677DF CRC64;
MAPSQFKTLM GSIRRKPSHA PDGKTDEQAY EKKMEEKTSL IHDLTHLGLK NTRTVAEAIT
TLASGEPMDD KDLLLEKGVA MLQSLPTNSG LSQTISNNFI GMLWKDLPHP PPTTAGPTAR
YRQPDGSGNN PWIPEMGKAG SPYSRSVPPM KPKGPNLPDP ELVFDQLLKR TGPFREHPSG
LNRLFFSFAT VVIHECFQTS RTNPLINETS SYVDLSTIYG NNANEQKRVR TYEQGRIFPD
SMASERIMMM PPGVVAVLLM FSRNHNHIAE NLLSVNEGGK YKDWDSLNDE QKAWQDEDIF
QLTRNINVGF FASVVLKDYV AAILNTPRAD SVWSLDLGGE IKNGGQRLER GSGNVVSVEF
AVLYHWHAAL SAADDKWMEY VIRSHLPDLQ SIDDVTAADF KKVMMTEGHK LMATPPKEWT
FGGLQRGPDG KFNDVELAEI IKDCIEEPAH AFGAHGTPAS LKIVDIMGQL QAREMFNVCT
MNEFRRYLNL KPYEDFEDWN PDKETARAAE LLYGHIENLE LYPGLMAEVT KPAMPGSGVC
PGHTTGRGIL DDAVALVRGD RFLSYDFNST TLSNWGFAKL GAIPAGAYGG MFPHLLFNAL
PGAWTGTSTY VLLPFYTPIA AKGILKGNKV LDQYDLDRPA SDKVVLGIHT HEGCKKVFED
RENFRVMYQT AIRKCTDGHD FLIGWDDAKR HDTRSSILHK VFFEEGFEAN LTKFFRTNVS
RLIKEKSLKY SSNRRSIDIV RDVTNVTPIL WLAERFAIPL KTKETPHGLM STPELFMIYL
VLFMYQSFNI IPANEWKLRE GAMKAAPALR AIFEAHLKTQ QGFKEGIVDW LAKGSAFEVG
PDADRIYHAL NDSKLPIGDL VGDCIGMGAP VAGNLTQQAS LLIDLYLSEG YEEYKDRIIE
LAHKDDAASE RELQGFVFEG MRHAGVVPGL PRVASKDVTV MDGSRGPINI KAGHTILIAT
SKAAMDPIQF PNPEKLNPHR PFKDYILLGH GLHFCFGARL VGTSLAATLK EVFKLKNIRR
ANGRQGHFSI VEHEFAGVKM RQYLDSNANE SPIPTTLTLE YDE
//
