PIOX_ORYSJ
ID PIOX_ORYSJ Reviewed; 618 AA.
AC Q2QRV3; Q0INH8; Q9M5J1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Alpha-dioxygenase PIOX {ECO:0000305};
DE EC=1.13.11.92 {ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
DE AltName: Full=Pathogen-induced oxygenase {ECO:0000303|PubMed:21790181};
GN Name=PIOX {ECO:0000303|PubMed:21790181};
GN OrderedLocusNames=Os12g0448900 {ECO:0000312|EMBL:BAT17016.1},
GN LOC_Os12g26290 {ECO:0000312|EMBL:ABA98060.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Matsui K., Koeduka T., Akakabe Y., Kajiwara T.;
RT "Fatty acid alpha-oxidases in rice plants.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-157; HIS-276; TYR-379;
RP HIS-382 AND SER-557.
RX PubMed=11909851; DOI=10.1074/jbc.m110420200;
RA Koeduka T., Matsui K., Akakabe Y., Kajiwara T.;
RT "Catalytic properties of rice alpha-oxygenase. A comparison with mammalian
RT prostaglandin H synthases.";
RL J. Biol. Chem. 277:22648-22655(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-311; TYR-379; ARG-558
RP AND ARG-559.
RX PubMed=18596034; DOI=10.1074/jbc.m804358200;
RA Koszelak-Rosenblum M., Krol A.C., Simmons D.M., Goulah C.C., Wroblewski L.,
RA Malkowski M.G.;
RT "His-311 and Arg-559 are key residues involved in fatty acid oxygenation in
RT pathogen-inducible oxygenase.";
RL J. Biol. Chem. 283:24962-24971(2008).
RN [7]
RP FUNCTION.
RX PubMed=21790181; DOI=10.1021/bi201016h;
RA Huff G.S., Doncheva I.S., Brinkley D.W., Angeles-Boza A.M., Mukherjee A.,
RA Cramer C.J., Roth J.P.;
RT "Experimental and computational investigations of oxygen reactivity in a
RT heme and tyrosyl radical-containing fatty acid alpha-(di)oxygenase.";
RL Biochemistry 50:7375-7389(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 10-618 IN COMPLEX WITH
RP HEXADECANOATE; HEME AND CALCIUM ION, AND COFACTOR.
RX PubMed=23934749; DOI=10.1002/pro.2327;
RA Zhu G., Koszelak-Rosenblum M., Malkowski M.G.;
RT "Crystal structures of alpha-dioxygenase from Oryza sativa: insights into
RT substrate binding and activation by hydrogen peroxide.";
RL Protein Sci. 22:1432-1438(2013).
CC -!- FUNCTION: Alpha-dioxygenase that catalyzes the primary oxygenation step
CC of a variety of 14-20 carbon fatty acids, containing up to three
CC unsaturated bonds, into their corresponding 2R-hydroperoxides
CC (PubMed:11909851, PubMed:18596034). Involved in the production of
CC oxylipins that function in cell signaling, wound healing, and
CC protection from infection (PubMed:11909851, PubMed:18596034).
CC {ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-saturated fatty acid + O2 = a (2R)-2-hydroperoxy fatty
CC acid; Xref=Rhea:RHEA:63508, ChEBI:CHEBI:15379, ChEBI:CHEBI:83955,
CC ChEBI:CHEBI:147340; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63509;
CC Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (2R,9Z,12Z)-2-
CC hydroperoxyoctadecadienoate; Xref=Rhea:RHEA:63860, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:149618; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63861;
CC Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 = (2R)-2-hydroperoxyhexadecanoate;
CC Xref=Rhea:RHEA:63836, ChEBI:CHEBI:7896, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:149616; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63837;
CC Evidence={ECO:0000269|PubMed:11909851, ECO:0000269|PubMed:18596034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (R)-2-hydroperoxy-
CC (9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:16329,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:76161;
CC EC=1.13.11.92; Evidence={ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16330;
CC Evidence={ECO:0000269|PubMed:18596034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + tetradecanoate = (2R)-2-hydroperoxytetradecanoate;
CC Xref=Rhea:RHEA:63856, ChEBI:CHEBI:15379, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:149617; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63857;
CC Evidence={ECO:0000269|PubMed:18596034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + octadecanoate = (2R)-2-hydroperoxyoctadecanoate;
CC Xref=Rhea:RHEA:63864, ChEBI:CHEBI:15379, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:149622; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63865;
CC Evidence={ECO:0000269|PubMed:18596034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 = (2R,9Z)-2-hydroperoxyoctadecenoate;
CC Xref=Rhea:RHEA:63868, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:149623; EC=1.13.11.92;
CC Evidence={ECO:0000269|PubMed:18596034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63869;
CC Evidence={ECO:0000269|PubMed:18596034};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:23934749};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:23934749};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:23934749};
CC Note=Binds 1 calcium ion per subunit. {ECO:0000269|PubMed:23934749};
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AF229813; AAF64042.2; -; mRNA.
DR EMBL; DP000011; ABA98060.2; -; Genomic_DNA.
DR EMBL; DP000011; ABG22010.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT17016.1; -; Genomic_DNA.
DR RefSeq; XP_015620386.1; XM_015764900.1.
DR PDB; 4KVJ; X-ray; 2.12 A; A=10-618.
DR PDB; 4KVK; X-ray; 1.98 A; A=10-618.
DR PDB; 4KVL; X-ray; 1.96 A; A=10-618.
DR PDBsum; 4KVJ; -.
DR PDBsum; 4KVK; -.
DR PDBsum; 4KVL; -.
DR AlphaFoldDB; Q2QRV3; -.
DR SMR; Q2QRV3; -.
DR STRING; 4530.OS12T0448900-01; -.
DR PeroxiBase; 4159; OsDiOx01.
DR PaxDb; Q2QRV3; -.
DR PRIDE; Q2QRV3; -.
DR EnsemblPlants; Os12t0448900-01; Os12t0448900-01; Os12g0448900.
DR GeneID; 4352160; -.
DR Gramene; Os12t0448900-01; Os12t0448900-01; Os12g0448900.
DR KEGG; osa:4352160; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_033051_0_0_1; -.
DR InParanoid; Q2QRV3; -.
DR OMA; AFAPWTK; -.
DR OrthoDB; 276568at2759; -.
DR BRENDA; 1.13.11.92; 4460.
DR Proteomes; UP000059680; Chromosome 12.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IEA:EnsemblPlants.
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:1902609; P:(R)-2-hydroxy-alpha-linolenic acid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0008219; P:cell death; IEA:EnsemblPlants.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEA:EnsemblPlants.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:EnsemblPlants.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEA:EnsemblPlants.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IEA:EnsemblPlants.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009627; P:systemic acquired resistance; IEA:EnsemblPlants.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Dioxygenase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Peroxidase;
KW Plant defense; Reference proteome.
FT CHAIN 1..618
FT /note="Alpha-dioxygenase PIOX"
FT /id="PRO_0000455382"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 162
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 311
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:23934749"
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:0000255|PROSITE-ProRule:PRU00298,
FT ECO:0000269|PubMed:23934749"
FT BINDING 479
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 483
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:23934749"
FT BINDING 599
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:23934749"
FT SITE 259
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MUTAGEN 157
FT /note="H->Q: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:11909851"
FT MUTAGEN 276
FT /note="H->Q: Reduces oxygenase activity 3.75-fold."
FT /evidence="ECO:0000269|PubMed:11909851"
FT MUTAGEN 311
FT /note="H->A: Reduces oxygenase activity 38-fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 311
FT /note="H->L: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 311
FT /note="H->Q: Reduces oxygenase activity 8.7-fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 379
FT /note="Y->F: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:11909851,
FT ECO:0000269|PubMed:18596034"
FT MUTAGEN 382
FT /note="H->Q: Reduces oxygenase activity 7.5-fold."
FT /evidence="ECO:0000269|PubMed:11909851"
FT MUTAGEN 557
FT /note="S->A: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:11909851"
FT MUTAGEN 558
FT /note="R->A: Reduces oxygenase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 558
FT /note="R->K: Reduces oxygenase activity 5.5-fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 558
FT /note="R->L: Slightly reduces oxygenase activity."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 559
FT /note="R->A: Reduces oxygenase activity 250-fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 559
FT /note="R->E: Reduces oxygenase activity 71-fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 559
FT /note="R->K: Reduces oxygenase activity more than 100-
FT fold."
FT /evidence="ECO:0000269|PubMed:18596034"
FT MUTAGEN 559
FT /note="R->L: Abolishes oxygenase activity."
FT /evidence="ECO:0000269|PubMed:18596034"
SQ SEQUENCE 618 AA; 70441 MW; BA0FD6A808E42A91 CRC64;
MGSGLFKPRV HPDLRDVFSK MSFFDKIGFL FIHAFDKRNL WHKVPVPIGL LYLNTRRTLL
EKYNLLAVGR SSHGALFDPK EFLYRTEDGK YNDPHNAEAG SQNTFFGRNM EPVDQQDELM
SPDPFVVATK LLARREYKDT GKQFNILAAA WIQFMVHDWM DHMEDTGQIG ITAPKEVANE
CPLKSFKFHP TKELPTNSDG IKIGHYNIRT AWWDGSAVYG NNEERAEKLR TYVDGKLVIG
DDGLLLHKEN GVALSGDIRN SWAGVSILQA LFVKEHNAVC DAIKEEHPNL SDEELYRYAK
LVTSAVIAKV HTIDWTVELL KTKTMRAAMR ANWYGLLGKK IKDTFGHIGG PILGGLVGLK
KPNNHGVPYS LTEEFTSVYR MHSLIPSTLK LRDPTGQPDA NNSPPCLEDI DIGEMIGLKG
EEQLSKIGFE KQALSMGYQA CGALELWNYP SFFRNLIPQN LDGTNRSDRI DLAALEVYRD
RERSVPRYNE FRRRLFLIPI KSWEDLTSDK DAIETIRAIY GDDVEKLDLL VGLMAEKKIK
GFAISETAFN IFILMASRRL EADRFFTSNF NEETYTKKGM QWVKTTEGLR DVINRHYPEI
TAKWMKSSSA FSVWDADY
