ID N1JA34_BLUG1 Unreviewed; 1058 AA.
AC N1JA34;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative fatty acid oxygenase PpoA {ECO:0000313|EMBL:CCU77021.1};
GN ORFNames=BGHDH14_bgh01025 {ECO:0000313|EMBL:CCU77021.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU77021.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU77021.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU77021.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU77021.1}.
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DR EMBL; CAUH01003268; CCU77021.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JA34; -.
DR STRING; 546991.N1JA34; -.
DR EnsemblFungi; BLGH_01776-mRNA-1; BLGH_01776-mRNA-1; BLGH_01776.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_0_0_1; -.
DR InParanoid; N1JA34; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000015441; 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:UP000015441}.
FT REGION 102..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
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 1058 AA; 117569 MW; 73FFCF247F33B083 CRC64;
MGPGQLKTLI GTIRRKPNRA PNTNEAAPPP EKTNLLHDIT HLGIKNTKTV AQAISTLASG
QPMNDKEELL ENGVEMLQSL PANSGLSEMV SNDFISMLWN DLPHPPPTQS GPSARFRKHD
GSGNNPWIPE MGKAGTPYSR SVPPMKPKGP NLPDPELVFE QLLKRNGPFR EHPSGLNRLF
FSFATIVIHE CFQSSRTNPW LNETSSYVDL STLYGNTENE QPRVRKYVNG LIYPDSIASE
RIMMMPPGVV AVLLLFSRNH NHIAENLLTI NEDGHYKEWE NLTEQEKKVQ DEEIFQIARN
INVGFFATIV LKDYVAAILN TPRANSTWSL DLGAEIKKGA TRIERGTGNV VSIEFVVLYH
WHAALSAADD KWMEDIIRSV FPDLKSIDDV TLEMYKEVMK SHGHKLMSTQ PKDWTFGGLE
RNADGHFDDY ELGELIKNCI EEPAHAFGAH GTPASLKVVD IMGQLQARDV FNVCTMNEFR
RYLNLTPYKS FEDWNEDKET ARAAELLYGN IENLELYPGL MAEVTKQPRA GSGVCPGQTT
GRGILDDAVA LVRGDRFLSY DFNSTTLTNW GVSKLATPSG GSYGGVLPEL LMKGIPGAWT
GTSIYALLPF YTPTAAKGIV KGNKAIAQYD LERPPSGMAV VGIHTHEGCK KAFEDRENFR
VMYMKAIKEC TGGFEFMLGW DDAARHDPRS TILYKAFFED GFEANISKFF AETTPRLIKE
SSLKYSGSKR SIDIVRDVTN VAPILWLAQR FAIPLKTMQK PRGILSVQEL FNVYLVLFIY
QSFNIIPANE WKLREGAHKA GAVLRSIHDA HLKTQQGITE GIVDWLAKDS AFEVGPEADR
LYHALNDTKL PVGDLSASCI LLAAPVAGNI TQQTSLLVDL YLSPGYEEYK ARIIELSHMD
SPEAERELQG FVYEGMRHAG VVPGVPRVVS KDITFIDGAR GPINLKAGHT VLIATGKAAM
DPVAFPNPEK LDPHRDFKSY SLLGHGMHFC FGARIVGSAM ASMLREIFKL KNIRRAPGKR
GQFSVVEHAL GGTQMRMYLN GSAKESPIPT TLTLEYDE
//
