ID A0A368UGH2_SOYBN Unreviewed; 607 AA.
AC A0A368UGH2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alpha-dioxygenase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLYMA_19G011800 {ECO:0000313|EMBL:RCW18780.1};
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:RCW18780.1};
RN [1] {ECO:0000313|EMBL:RCW18780.1, ECO:0000313|EnsemblPlants:RCW18780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:RCW18780};
RC TISSUE=Callus {ECO:0000313|EMBL:RCW18780.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EMBL:RCW18780.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:RCW18780.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:RCW18780}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:RCW18780};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR EMBL; CM000852; RCW18780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368UGH2; -.
DR EnsemblPlants; RCW18780; RCW18780; GLYMA_19G011800.
DR Gramene; RCW18780; RCW18780; GLYMA_19G011800.
DR OMA; MARVRTY; -.
DR Proteomes; UP000008827; Chromosome 19.
DR ExpressionAtlas; A0A368UGH2; baseline.
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: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:SF11; ALPHA-DIOXYGENASE 1; 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:UP000008827}.
FT BINDING 357
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 607 AA; 69252 MW; F24499994A8021D6 CRC64;
MWHTQIVHSI DKLGLWHRLP VFFGLLYLGI RRHLQQQYNL FNVGTTPVGI RFNPSDFPYR
TDDGKYNDPF NEVAGSQGSF FGRNILPVDH KNKLLKPDPM VVATKLLARR TYKDTGKQFN
VIAASWIQFM IHDWIDHLED TNQIELIAPR EVASQCPLKS FKFYKTKEIP TGFFEIKSGS
SNIRTPWWDG SVIYGSNREV LEKVRTFKDG KIKISKDGHL LHNENGTAIS GDVRNSWAGV
STLQALFTQE HNAVCDALKS NYPHLEDEEV YRHARLVTSA VIAKVHTIDW TVELLKTDTL
LAAMHANWYG LLGKTFKDTF GHVGGAALGG LVGLKRPENH GVTYSLTEEF VSAYRIHSLL
PDNLQLRDIS ATPGPNKSPP LIKEIPMKNL IGVQGEEALT KIGVERQLVS MGHQACGALE
LWNYPLWLRD LVPQNIDGTE RKDHIDLAAL EIYRDRERSV ARYNQFRRAL LLIPISKWED
LTDDQEAIQV LEEVYGDDIE ELDLLVGLMA EKKIKGFAIS ETAFTIFIFM SSRRLEADRF
FTSNFNEDAY TKKGLEWVNT TESLKNVIDR HYPEITHKWL NSSSVFSVWN SPPNTQNPIP
LYLRVPH
//
