PIOX_TOBAC
ID PIOX_TOBAC Reviewed; 643 AA.
AC A0A1S3ZX38; O82031;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Alpha-dioxygenase PIOX {ECO:0000305};
DE EC=1.13.11.92 {ECO:0000269|PubMed:9724698};
DE AltName: Full=Pathogen-induced oxygenase {ECO:0000303|PubMed:9724698};
GN Name=PIOX {ECO:0000303|PubMed:9724698};
GN ORFNames=LOC107791409 {ECO:0000312|RefSeq:XP_016468957.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=9724698; DOI=10.2307/3870616;
RA Sanz A., Moreno J.I., Castresana C.;
RT "PIOX, a new pathogen-induced oxygenase with homology to animal
RT cyclooxygenase.";
RL Plant Cell 10:1523-1537(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
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:9724698). Involved in the production of oxylipins that function
CC in cell signaling, wound healing, and protection from infection
CC (PubMed:9724698). {ECO:0000269|PubMed:9724698}.
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:9724698};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63509;
CC Evidence={ECO:0000269|PubMed:9724698};
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:9724698};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16330;
CC Evidence={ECO:0000269|PubMed:9724698};
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:9724698};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63861;
CC Evidence={ECO:0000269|PubMed:9724698};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q9SGH6};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q9SGH6};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9SGH6};
CC Note=Binds 1 calcium ion per subunit. {ECO:0000250|UniProtKB:Q9SGH6};
CC -!- INDUCTION: Induced by the elicitor harpin (HrpN) from Erwinia amylovora
CC and infection with E.amylovora (PubMed:9724698). Induced by infection
CC with the bacterial pathogens Pseudomonas syringae pv syringae and
CC Pseudomonas syringae pv tabaci (PubMed:9724698). Induced by salicylate
CC (SA), wounding, jasmonate (JA), paraquat and 3-amino-1,2,4-triazole
CC (3AT) (PubMed:9724698). {ECO:0000269|PubMed:9724698}.
CC -!- SIMILARITY: Belongs to the peroxidase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00298}.
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DR EMBL; AJ007630; CAA07589.1; -; mRNA.
DR PIR; T03631; T03631.
DR RefSeq; XP_016468957.1; XM_016613471.1.
DR SMR; A0A1S3ZX38; -.
DR STRING; 4097.A0A1S3ZX38; -.
DR PeroxiBase; 4117; NtDiOx01-1A.
DR GeneID; 107791409; -.
DR KEGG; nta:107791409; -.
DR OMA; MARVRTY; -.
DR OrthoDB; 276568at2759; -.
DR BRENDA; 1.13.11.92; 3645.
DR Proteomes; UP000084051; Unplaced.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; -; 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 Calcium; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Peroxidase; Plant defense; Reference proteome.
FT CHAIN 1..643
FT /note="Alpha-dioxygenase PIOX"
FT /id="PRO_0000455381"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 172
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 392
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 BINDING 489
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT BINDING 493
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q9SGH6"
FT SITE 269
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 24
FT /note="F -> L (in Ref. 1; CAA07589)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="K -> R (in Ref. 1; CAA07589)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> K (in Ref. 1; CAA07589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 73453 MW; E997AE788933B6FF CRC64;
MSLVMDSLKN LLLSPLRGFI HKDFHDIFER MTLLSKLLFL IVHLVDKLNL WHRLPVLLGL
LYLGARRHLH QEYNLINVGK TPIGVRSNPA DHPYRTADGK YNDPFNEGAG SELSFFGRNM
LPVDQHNQLK KPDPMVVATK LLARRNFVDT GKQFNMIAAS WIQFMIHDWI DHLEDTKQIE
LKAAEEVASQ CPLKSFKFFK TKEIPTGFYE IKTGHLNTRT PWWDGSAIYG SNAEVLKKVR
TFKDGKLKLS ADGLLEIDKN GKIISGDVRN TWAGLSALQA LFVQEHNSVC DALKKEYPEL
EEEDLYRHAR LVTSAVIAKV HTIDWTVELL KTDTLLAGMR ANWYGLLGKK FKDTFGHVGG
SILGGFVGMK KPENYGVPYS LTEEFTSVYR MHQLLPDKLQ LRNIDATPGP NKSLPLTNEI
PLEDLIGGKG EENLSKIGFT KQMVSMGHQA CGALELWNYP VWMRDLIPQD VDGTDRPDHI
DLAALEIYRD RERSVARYNE FRRGMLQIPI SKWEDLTDDE EVINTLGEVY GDDVEELDLM
VGMAAEKKIK GFAISETAFF IFLVMASRRL EADRFFTSNY NEETYTKKGL EWVNTTESLK
DVLDRHYPEI TEKWMNSSSA FSVWDSTPQP HNPIPLYFRV PPQ
