PXG1_AVESA
ID PXG1_AVESA Reviewed; 249 AA.
AC G1JSL4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Peroxygenase 1;
DE Short=AsPXG1;
DE EC=1.11.2.3;
OS Avena sativa (Oat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Aveninae; Avena.
OX NCBI_TaxID=4498;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. CDC Dancer;
RX PubMed=21784965; DOI=10.1104/pp.111.178822;
RA Meesapyodsuk D., Qiu X.;
RT "A peroxygenase pathway involved in the biosynthesis of epoxy Fatty acids
RT in oat.";
RL Plant Physiol. 157:454-463(2011).
RN [2]
RP PROTEIN SEQUENCE OF 10-35, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16956885; DOI=10.1074/jbc.m605395200;
RA Hanano A., Burcklen M., Flenet M., Ivancich A., Louwagie M., Garin J.,
RA Blee E.;
RT "Plant seed peroxygenase is an original heme-oxygenase with an EF-hand
RT calcium binding motif.";
RL J. Biol. Chem. 281:33140-33151(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=14535881; DOI=10.1046/j.1365-313x.2003.01865.x;
RA Lequeu J., Fauconnier M.L., Chammai A., Bronner R., Blee E.;
RT "Formation of plant cuticle: evidence for the occurrence of the
RT peroxygenase pathway.";
RL Plant J. 36:155-164(2003).
CC -!- FUNCTION: Calcium-binding peroxygenase involved in cutin monomers
CC biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation
CC reactions that can proceede competitively, although in favor of the
CC sulfoxidation. Can only use unsaturated fatty acids with double bonds
CC in the cis configuration as substrates. The preferred substrate is
CC oleic acid and is inactive toward ricinoleic acid. Free fatty acid and
CC fatty acid methyl esters are effective substrate forms, but not
CC phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are
CC preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors.
CC {ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885,
CC ECO:0000269|PubMed:21784965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
CC Evidence={ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885,
CC ECO:0000269|PubMed:21784965};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by beta-mercaptoethanol and
CC organophosphorothioates such as parathion or terbufos.
CC {ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:21784965}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.07 uM for 9-HPOD {ECO:0000269|PubMed:21784965};
CC KM=10.42 uM for 9-HPOT {ECO:0000269|PubMed:21784965};
CC KM=25.18 uM for 13-HPOD {ECO:0000269|PubMed:21784965};
CC KM=7.25 uM for 13-HPOT {ECO:0000269|PubMed:21784965};
CC KM=215.76 uM for cumene hydroperoxide {ECO:0000269|PubMed:21784965};
CC Vmax=214.04 pmol/sec/mg enzyme toward 9-HPOD
CC {ECO:0000269|PubMed:21784965};
CC Vmax=188.69 pmol/sec/mg enzyme toward 9-HPOT
CC {ECO:0000269|PubMed:21784965};
CC Vmax=306.57 pmol/sec/mg enzyme toward 13-HPOD
CC {ECO:0000269|PubMed:21784965};
CC Vmax=173.49 pmol/sec/mg enzyme toward 13-HPOT
CC {ECO:0000269|PubMed:21784965};
CC Vmax=883.34 pmol/sec/mg enzyme toward cumene hydroperoxide
CC {ECO:0000269|PubMed:21784965};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:21784965};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:21784965};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane. Lipid droplet.
CC -!- TISSUE SPECIFICITY: Expressed only in developing seeds. Not detected in
CC roots, leaves, glumes and germinating seeds.
CC {ECO:0000269|PubMed:21784965}.
CC -!- DOMAIN: Transmembrane regions are predicted by sequence analysis tools,
CC but these regions probably constitute hydrophobic domains associated to
CC phospholipids.
CC -!- DOMAIN: The proline-knot motif (124-133) may be involved in targeting
CC to lipid bodies.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR EMBL; JN390966; AEL03786.1; -; mRNA.
DR AlphaFoldDB; G1JSL4; -.
DR KEGG; ag:AEL03786; -.
DR BRENDA; 1.11.2.3; 588.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0102070; F:18-hydroxyoleate peroxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
DR InterPro; IPR007736; Caleosin-related.
DR PANTHER; PTHR31495; PTHR31495; 1.
DR Pfam; PF05042; Caleosin; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW Lipid droplet; Membrane; Metal-binding; Microsome; Oxidoreductase.
FT CHAIN 1..249
FT /note="Peroxygenase 1"
FT /id="PRO_0000415559"
FT DOMAIN 68..103
FT /note="EF-hand"
FT MOTIF 124..133
FT /note="Proline-knot"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
SQ SEQUENCE 249 AA; 28107 MW; B7930FBDBA745A7C CRC64;
MAEDAVVSDA VVVSDAMSSV AKGAPVTAQR PVRDDLEKHI PKPYLARALV AVDVNNPEGT
KGGRHEHGQK SVLQQHVSFF DQNGDGIIYP WETFRGLRRL GFNLIVSFIV AIGIHTGLSY
PTLPTWRPSL LFPVYIDRIH KAKHGSDTAT FDTEGRFMPV NFENIFSKNA RSQPDKLTLR
EIWMMTNDHR LAYDPFGWVA NKGEWILLYM LAKDDEGYLP KEAIRGVYDG SLFEFLAEQR
TKKAHGKQH
