ID D7SJ80_VITVI Unreviewed; 634 AA.
AC D7SJ80;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Alpha-dioxygenase 2 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_17s0000g02700 {ECO:0000313|EMBL:CBI15541.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI15541.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR EMBL; FN594950; CBI15541.3; -; Genomic_DNA.
DR RefSeq; XP_002281357.1; XM_002281321.4.
DR AlphaFoldDB; D7SJ80; -.
DR STRING; 29760.D7SJ80; -.
DR PaxDb; 29760-VIT_17s0000g02700-t01; -.
DR EnsemblPlants; Vitvi17g00237_t001; Vitvi17g00237_P001; Vitvi17g00237.
DR GeneID; 100260995; -.
DR Gramene; Vitvi17g00237_t001; Vitvi17g00237_P001; Vitvi17g00237.
DR KEGG; vvi:100260995; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_033051_0_0_1; -.
DR InParanoid; D7SJ80; -.
DR OMA; SCNHLER; -.
DR OrthoDB; 1086441at2759; -.
DR Proteomes; UP000009183; Chromosome 17.
DR ExpressionAtlas; D7SJ80; baseline and differential.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
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:UP000009183}.
FT BINDING 382
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 634 AA; 72485 MW; B51ABE6AFEF70C71 CRC64;
MAFSKSSSSF IHPQLLHIVA KMTLFDTFLF YIVHFVDKLG VWHRLPVLLG LAYLGIRRHL
HQRYNLLHVG GVNGGRYDTE EFCYRTADGK CNHPIDDQIG SQGTLFGRNM PPSTSSYRLL
EPHPTVVATK LLARKKFIDN GKQFNLIACS WVQFMIHDWI DHMEDTQQIE IKAPSDIASG
CPLKSFKFFK SKSIPTGSPH MEDGFLNTRT PWWDGSVIYG NNDDGMRRVR TFKDGKLKIS
NDGLLEHDGK GIPISGDVRN CWAGFSLLQA LFVKEHNAVC DMLKVHHPEF DDERLYRHAR
LVTSAVIAKI HTIDWTVELL KTDTLLAGMR INWYGFMGKK FKDSFGHILG PILSGLVGLK
KPRDHGVPYS LTEEFVSVYR MHALLPDELH IRDTNSSNTA SEGECPPLIE EVPMREMVGL
EGEKRLSKIG MEKMMVSMGH QASGAMALWN YPSWMRNLVA HDVNGEDRPD LVDMAALEIY
RDRERGVARY NEFRRNLLMI PISKWEDLTD DEKVVEALCE VYGDDVEKLD LLVGLHAEKK
IKGFAICETA FFIFLLIASR RLEADRFFTT NFNSQTYTRS GLDWVNKTET LQDVLDRHFP
DMTKKWMRCS SAFSVWDSTP TPTNYIPLYL RPAP
//
