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Database: UniProt/TrEMBL
Entry: M5WDX5_PRUPE
LinkDB: M5WDX5_PRUPE
Original site: M5WDX5_PRUPE 
ID   M5WDX5_PRUPE            Unreviewed;       633 AA.
AC   M5WDX5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Alpha-dioxygenase 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PRUPE_5G230200 {ECO:0000313|EMBL:ONI09302.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI09302.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI09302.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR   EMBL; CM007655; ONI09302.1; -; Genomic_DNA.
DR   RefSeq; XP_007210768.1; XM_007210706.1.
DR   AlphaFoldDB; M5WDX5; -.
DR   STRING; 3760.M5WDX5; -.
DR   EnsemblPlants; ONI09302; ONI09302; PRUPE_5G230200.
DR   GeneID; 18777310; -.
DR   Gramene; ONI09302; ONI09302; PRUPE_5G230200.
DR   KEGG; pper:18777310; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_033051_0_0_1; -.
DR   OMA; SCNHLER; -.
DR   OrthoDB; 1086441at2759; -.
DR   Proteomes; UP000006882; Chromosome g5.
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:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09818; PIOX_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR034815; A_dioxygenase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11903:SF25; ALPHA-DIOXYGENASE 2; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882}.
FT   BINDING         383
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   633 AA;  72643 MW;  4F3CFB877E8A22E6 CRC64;
     MAFFLSSCST FVHPQLQPIV AKMTLLDTLF FYVIHFVDKL GIWHRLPVFM GLAYLGIRRH
     LHQRYNLLHV GRINGQKYDT ERLSYRTADG TCNHPHDHLV GSQGTCFGRN MPPSTSPYGL
     LEPHPAIVAS KLLARKKFVD NGKQFNMIAC SWIQFMIHDW VDHLEDTEQV EIKAPEEIAT
     GCPLKSFKFY KTKKVPTAST SSDSDCLNAR TPWWDGSVIY GNNMEGMQRV RTFKDGKLKI
     SGDGLLEHDE NGIPISGDVR NCWAGFSLLQ ALFAKEHNAA CDMLKVHYPD LDDEKLYRHA
     RLVTSAVIAK IHTIDWTVEL LKTDTLLAGM RINWYGFLGK RFKDLHGHIL GPILNGLVGL
     KKPRDHGVPY SLTEEFVSVY RMHALLPDKL ILRDIESTAS EDKCPPILEE VLMRDMAGKE
     GERRLSTIGM EQMLVSMGHQ ACGAITLWNY PSWMRNLIAH DVNGEDRADP VDMAALEIYR
     DRERGVARYN EFRRNLLMIP INKWEDLTDD KEVVEALKEV YGDDVEKLDL QVGLHAEKKI
     KGFAISETAF FIFLLIASRR LEADRFFTTN FNSKTYTEKG LEWVNKTETL KDVIDRHFPE
     MTRRWMKCSS AFSVWDWEPN PESYIPLYLR PAP
//
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