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Database: UniProt/TrEMBL
Entry: R0HV90_9BRAS R0IAX1_9BRAS
LinkDB: R0HV90_9BRAS R0IAX1_9BRAS
Original site: R0HV90_9BRAS R0IAX1_9BRAS 
ID   R0HV90_9BRAS            Unreviewed;       561 AA.
AC   R0HV90;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Alpha-dioxygenase 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CARUB_v10019959mg {ECO:0000313|EMBL:EOA33764.1};
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:EOA33764.1, 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).
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DR   EMBL; KB870806; EOA33764.1; -; Genomic_DNA.
DR   RefSeq; XP_006300866.1; XM_006300804.1.
DR   AlphaFoldDB; R0HV90; -.
DR   Proteomes; UP000029121; 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:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
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:ARBA00023160};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029121}.
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   561 AA;  63831 MW;  A039E2000D8B36CA CRC64;
     MGFSPSSSWF LDPQLHHFVS KMSVFDAFLF YIVHLVDKLD LWHRFPVLLG VAYLGMRRHL
     HQRYNLVHVG GINGQSYDTD EFCYRTADGK CNHPSDDSIG SQGSFIGRNM PPSTSQYGIL
     DPHPSVVATK LLARKRFIDN GDQFNMIACS WIQFMIHDWV DHLEDTDQIE LEAPEEVASG
     CPLKSFKFLK TKKVPTDDHH KSGAVNTRTP WWDGSVVYGN DEAGMRRVRV FKDGKLKISG
     DGLLELDERG VPISGDIRNS WSGFSLLQAL FVKEHNAVCD MLKERYPEFD DEKLYRTARL
     VTAAVIAKVH TIDWTIELLK TDTLTAGMRI NWYGFLGKKV KDMVGARFGP ILSGLVGLKK
     PKDHGVPYSL TEEFVSVYRM HCLLPDTLIL RDMKSENVDK SNPAIEREIP MTELIGKAGG
     KAGSRIGFEQ LLVSMGHQSC GALTLWNYPN WMRNLVAQDI DGEDRPHLID MAALEIYRDR
     ERGVPRYNEF RKNLLMSPIS KWEDLTDDYE AIEVLREVYG DDIEKLDLNV GLHAEKKIKG
     FAISETAFFI FLLVASRFLN F
//
ID   R0IAX1_9BRAS            Unreviewed;       631 AA.
AC   R0IAX1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Alpha-dioxygenase 2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CARUB_v10019959mg {ECO:0000313|EMBL:EOA33763.1};
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:EOA33763.1, 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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CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB870806; EOA33763.1; -; Genomic_DNA.
DR   RefSeq; XP_006300865.1; XM_006300803.1.
DR   AlphaFoldDB; R0IAX1; -.
DR   STRING; 81985.R0IAX1; -.
DR   GeneID; 17895917; -.
DR   KEGG; crb:17895917; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   OrthoDB; 1086441at2759; -.
DR   Proteomes; UP000029121; 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: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:UP000029121}.
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;  71991 MW;  BB03AF32309EB766 CRC64;
     MGFSPSSSWF LDPQLHHFVS KMSVFDAFLF YIVHLVDKLD LWHRFPVLLG VAYLGMRRHL
     HQRYNLVHVG GINGQSYDTD EFCYRTADGK CNHPSDDSIG SQGSFIGRNM PPSTSQYGIL
     DPHPSVVATK LLARKRFIDN GDQFNMIACS WIQFMIHDWV DHLEDTDQIE LEAPEEVASG
     CPLKSFKFLK TKKVPTDDHH KSGAVNTRTP WWDGSVVYGN DEAGMRRVRV FKDGKLKISG
     DGLLELDERG VPISGDIRNS WSGFSLLQAL FVKEHNAVCD MLKERYPEFD DEKLYRTARL
     VTAAVIAKVH TIDWTIELLK TDTLTAGMRI NWYGFLGKKV KDMVGARFGP ILSGLVGLKK
     PKDHGVPYSL TEEFVSVYRM HCLLPDTLIL RDMKSENVDK SNPAIEREIP MTELIGKAGG
     KAGSRIGFEQ LLVSMGHQSC GALTLWNYPN WMRNLVAQDI DGEDRPHLID MAALEIYRDR
     ERGVPRYNEF RKNLLMSPIS KWEDLTDDYE AIEVLREVYG DDIEKLDLNV GLHAEKKIKG
     FAISETAFFI FLLVASRRLE ADRFFTTNFN EKTYTKEGLE WVNTTETLKD VIDRHFPSLT
     KQWMRCSSAF SVWGSDPNPA TWVPLYLRTA P
//
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