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). CC --------------------------------------------------------------------------- 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; 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}; CC --------------------------------------------------------------------------- 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 //