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Database: UniProt
Entry: R0I162_9BRAS
LinkDB: R0I162_9BRAS
Original site: R0I162_9BRAS 
ID   R0I162_9BRAS            Unreviewed;       645 AA.
AC   R0I162;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Alpha-dioxygenase 1 {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=CARUB_v10013184mg {ECO:0000313|EMBL:EOA30078.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA30078.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR   EMBL; KB870807; EOA30078.1; -; Genomic_DNA.
DR   RefSeq; XP_006297180.1; XM_006297118.1.
DR   AlphaFoldDB; R0I162; -.
DR   STRING; 81985.R0I162; -.
DR   GeneID; 17892716; -.
DR   KEGG; crb:17892716; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   OrthoDB; 1086441at2759; -.
DR   Proteomes; UP000029121; 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: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:UP000029121}.
FT   BINDING         395
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:EOA30078.1"
SQ   SEQUENCE   645 AA;  73939 MW;  D9BCDB9B5BF6695A CRC64;
     PQKLKRMKLI TSLISSILLK FIHKDFHEIY SRMSLLDRLI LLVVHAVDKM VPWHKLPVFL
     GLAYLEARRH LHQEYNLLNV GQTPVGTRFD PANFPYRTAD GKFNDPFNEG VGSQNSFFGR
     NCPPVDQKTK LLRPDPMVVA TKLLGRRKFI DTGKQFNMIA ASWIQFMIHD WIDHLEDTHQ
     IELVAPREVA NQCPLRSFRF FKTKEVPTGF FDIKTGSQNI RTPWWDSSVI YGSNSKTMDR
     VRTYKDGKLK ISEETGLLLH DKDGIAISGD VRNSWVGVSA LQALFIKEHN AVCDALKDDD
     NDLEDEDLYR HARLVTSAVI AKIHTIDWTT QLLKTDTLLA GMRANWYGVL GKKFKDSFGH
     AGSSILGGVV GMKKPKNHGV PYSLTEDFAS VYRMHSLLPD QLQMRDIDDE PGTNKSLPLI
     KEISMSHLIG LKGEQTMSQI GFTKLMVSMG HQASGALELM NYPLWFRDII PHDHNGQERS
     DHVDLAALEI YRDRERSVPR YNDFRRAMFM IPITKWEDLT ADKDAIEVLD DVYDGDVEEL
     DLLVGLMAEK KIKGFAISET AFYIFLLMAT RRLEADRFFT SDFNETVYTK KGLKWVNTTE
     SLKDVFDRHY PEMTDKWMNS ESAFSVWDSP PVTKNPIPLY LRIPS
//
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