DOX2_ARATH
ID DOX2_ARATH Reviewed; 631 AA.
AC Q9C9U3; F4HRY9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Alpha-dioxygenase 2;
DE Short=Alpha DOX2;
DE EC=1.14.99.-;
DE AltName: Full=Fatty acid dioxygenase AlphaDOX2;
DE Flags: Precursor;
GN Name=DOX2; Synonyms=DIOX2; OrderedLocusNames=At1g73680; ORFNames=F25P22.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17369372; DOI=10.1105/tpc.106.046052;
RA Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L.,
RA Hamberg M., Castresana C.;
RT "Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate
RT lateral root development and defense responses through a specific signaling
RT cascade.";
RL Plant Cell 19:831-846(2007).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19759339; DOI=10.1104/pp.109.145094;
RA Bannenberg G., Martinez M., Rodriguez M.J., Lopez M.A., Ponce de Leon I.,
RA Hamberg M., Castresana C.;
RT "Functional analysis of alpha-DOX2, an active alpha-dioxygenase critical
RT for normal development in tomato plants.";
RL Plant Physiol. 151:1421-1432(2009).
CC -!- FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation of
CC fatty acids into oxylipins. May be involved in the senescence process.
CC {ECO:0000269|PubMed:19759339}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000305|PubMed:19759339};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C9U3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C9U3-2; Sequence=VSP_044438;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings (cotyledons, young leaves,
CC and hypocotyls), flowers, siliques and old leaves.
CC {ECO:0000269|PubMed:17369372, ECO:0000269|PubMed:19759339}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during senescence
CC induced by detachment of leaves. In flowers, expressed in anthers and
CC ovules prior to fertilization, and in siliques, present in developing
CC seeds. {ECO:0000269|PubMed:19759339}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AC012679; AAG52078.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35496.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35497.1; -; Genomic_DNA.
DR EMBL; AY081283; AAL91172.1; -; mRNA.
DR EMBL; AY128743; AAM91143.1; -; mRNA.
DR PIR; H96763; H96763.
DR RefSeq; NP_001185393.1; NM_001198464.1. [Q9C9U3-2]
DR RefSeq; NP_177509.1; NM_106027.3. [Q9C9U3-1]
DR AlphaFoldDB; Q9C9U3; -.
DR SMR; Q9C9U3; -.
DR STRING; 3702.AT1G73680.2; -.
DR PeroxiBase; 3378; AtDiOx02.
DR PaxDb; Q9C9U3; -.
DR PRIDE; Q9C9U3; -.
DR ProteomicsDB; 222141; -. [Q9C9U3-1]
DR EnsemblPlants; AT1G73680.1; AT1G73680.1; AT1G73680. [Q9C9U3-1]
DR EnsemblPlants; AT1G73680.2; AT1G73680.2; AT1G73680. [Q9C9U3-2]
DR GeneID; 843703; -.
DR Gramene; AT1G73680.1; AT1G73680.1; AT1G73680. [Q9C9U3-1]
DR Gramene; AT1G73680.2; AT1G73680.2; AT1G73680. [Q9C9U3-2]
DR KEGG; ath:AT1G73680; -.
DR Araport; AT1G73680; -.
DR TAIR; locus:2027799; AT1G73680.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_033051_0_0_1; -.
DR InParanoid; Q9C9U3; -.
DR OMA; RYPHIDE; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; Q9C9U3; -.
DR PRO; PR:Q9C9U3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9U3; baseline and differential.
DR Genevisible; Q9C9U3; AT.
DR GO; GO:0051213; F:dioxygenase activity; IDA:TAIR.
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:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:TAIR.
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; -; 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 Pfam; PF03098; An_peroxidase; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Dioxygenase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
KW Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..631
FT /note="Alpha-dioxygenase 2"
FT /id="PRO_0000420285"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:19759339"
FT BINDING 157
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:0000305|PubMed:19759339"
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:0000305|PubMed:19759339"
FT SITE 258
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 119..125
FT /note="ILDPHPS -> FFCQYFFFPENLEKKI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044438"
SQ SEQUENCE 631 AA; 72458 MW; 4EA935DC544017F6 CRC64;
MGFSPSSSWF LHPQLHHVVS KMSYFDAFLF YIVHLVDKLG LWHRFPVLLG VAYLGLRRHL
HQRYNLVHVG PINGQGYDTD EFCYRTADGK CNHPSDNTIG SQGSFIGRNM PPSTSQYGIL
DPHPSVVATK LLARKRFIDN GDQFNVIACS WIQFMIHDWV DHLEDTHQIE LEAPEEVASG
CPLKSFKFLR TKKVPTDDHH KSGAVNTRTP WWDGSVIYGN DETGMRRVRV FKDGKLKISG
DGLLERDERG VPISGDIRNS WSGFSLLQAL FVKEHNSVCD MLKERYPDFD DEKLYRTARL
VTAAVIAKVH TIDWTIELLK TDTLTAGMRI NWYGFFGKKV KDMVGARFGP LFSGLVGLKK
PNDHGVPYSL TEEFVSVYRM HCLLPETLIL RDMNSENVDK ENPAIEREIP MTELIGKKAG
EKASKLGFEQ LLVSMGHQSC GALTLWNYPN WMRNLVAQDI DGEDRPHLID MAALEIYRDR
ERGVPRYNEF RKNLLMSPIS KWEELTDDEE AIKVLREVYE DDIEKLDLNV GLHAEKKIKG
FAISETAFFI FLLVASRRLE ADRFFTTNFN EKTYTKEGLE WVNTTETLKD VIDRHFPRLT
DQWMRCSSAF SVWGSDPNPK NWVPLYLRSA P
