ID A0A078IEX1_BRANA Unreviewed; 631 AA.
AC A0A078IEX1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=BnaA02g16520D protein {ECO:0000313|EMBL:CDY47743.1};
GN Name=BnaA02g16520D {ECO:0000313|EMBL:CDY47743.1};
GN ORFNames=GSBRNA2T00088021001 {ECO:0000313|EMBL:CDY47743.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY47743.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY47743.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR EMBL; LK032732; CDY47743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078IEX1; -.
DR STRING; 3708.A0A078IEX1; -.
DR PaxDb; 3708-A0A078IEX1; -.
DR EnsemblPlants; CDY47743; CDY47743; GSBRNA2T00088021001.
DR Gramene; CDY47743; CDY47743; GSBRNA2T00088021001.
DR OMA; SEPCYLA; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
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:SF29; 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:UP000028999}.
FT BINDING 381
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 631 AA; 72315 MW; C01F8410A7BC26C8 CRC64;
MAFSLSSSWF LHPELHHVVS KMSFFDSFLF YIVHLVDKLG LWHRFPVLLG VAYLGIRRHL
HQRYNLIHVG GINGQGYDTD EFSYRTADGK CNHPSDDSIG SQGTFIGRNM PPCTSQYGIL
DPHPSVVATK LLARKRFIDN GDQFNVIACS WIQFMIHDWV DHLEDTNQIE LEAPEGVASG
CPLKSFKFFR TKKVLSGDHH KSGAVNTRTP WWDGSVIYGN DEAGMRRVRV FKDGKLRISG
DGLLERDERG VPISGDIRNS WSGFSLLQAL FVKEHNSVCE MLKERYPDFD DEKLYRTARL
VTAAVIAKIH TIDWTLELLK TDTLTAGMRI NWYGFLGKKV KDKIGARFGP ILSGLVGLKK
PRDHGVPYSL TEEFVSVYRM HCLLPDTLIL RDMRPENVDK ENPAIEREVP MTKLIGKEGG
KTDSRIGFEQ LLVSMGHQSC GALTLWNYPN WMRNLVAQDI DGEDRPNLID MAALEIYRDR
ERGVPRYNEF RKNLLMSPIK NWEDLTDDEE AIHALKEVYE DDIDKVDVNV GLHAEKKIKG
FAISETAFFI FLLVASRRLE ADRFFTTNFN DRTYTKEGLE WVNTTETLKD VIDRHFPNLT
NQWMRCTSAF SVWSSDPDPT NWLPLYLRSA P
//
