ID A4PRI0_MEDTR Unreviewed; 584 AA.
AC A4PRI0;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Haem peroxidase {ECO:0000313|EMBL:ABP02610.1};
DE Flags: Fragment;
GN ORFNames=MtrDRAFT_AC139526g53v2 {ECO:0000313|EMBL:ABP02610.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:ABP02610.1};
RN [1] {ECO:0000313|EMBL:ABP02610.1}
RP NUCLEOTIDE SEQUENCE.
RA Shaull S., Lin S., Dixon R., May G., Sumner L., Gonzales B., Cook D.,
RA Kim D., Roe B.A.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP02610.1}
RP NUCLEOTIDE SEQUENCE.
RG The International Medicago Genome Annotation Group;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR EMBL; AC139526; ABP02610.1; -; Genomic_DNA.
DR AlphaFoldDB; A4PRI0; -.
DR PeroxiBase; 5140; MtDiOx02.
DR EnsemblPlants; AET05548; AET05548; MTR_8g106800.
DR Gramene; AET05548; AET05548; MTR_8g106800.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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 Peroxidase {ECO:0000313|EMBL:ABP02610.1}.
FT BINDING 337
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABP02610.1"
SQ SEQUENCE 584 AA; 67024 MW; 953241213075C7FC CRC64;
PVLLGAIYLG IRRHLHFRYN LLHVGGVSGN NYDTQHYAYR TPAGTCNHPD DHLIGSQGTI
IGRNMPPTTL NYGLLDPHPA VVTSKLLARK SFIDTGKQFN MIACSWIQFM IHDWIDHLED
TEQVEIGVPD GYSSGCPLKT FKFFKTKKFQ TGSSHMKFGF QNTRTPWWDG SVIYGNNEKG
MGRVRTFKEG KLKISEDGLL EHDEKGIPVS GDVRNSWAGY SLLQALFIKE HNAVCDMLKE
HYPDFDDEQL YRYARLVTSA VIAKIHTIDW TVELLKTDTL LASMRINWYG FLGKKFKDSF
GNILGPELSG LVGLKEPRDH GVPYSLTEEF TSVYRMHALL PEELVLRNIK PTTGEDKCPS
ILEKVPMTEM IGKQGEKRLS KIGMEQMLVS MGHQPCGAIT LWNFPTWLRN LIAHDIDGEE
RPDPVDIATM EVYRDRERGV ARYNEFRRNM LMIPISKWED LTDDEEVNEA LKEVYDDDVE
KLDLIVGLHA EKKIKGFAIS ETAFFIFVIM ASRRLEADRF FTTNFNSKTY TNQGFEWVNK
TESLKDVIDR HFPEMTKNWM TSSSAFSVWD SMPDPKKYIP LYLR
//
