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Peroxygenase 1 (AsPXG1) (EC 1.11.2.3)

 PXG1_AVESA              Reviewed;         249 AA.
G1JSL4;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 1.
27-SEP-2017, entry version 23.
RecName: Full=Peroxygenase 1;
Short=AsPXG1;
EC=1.11.2.3;
Avena sativa (Oat).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Poodae; Poeae; Aveninae; Avena.
NCBI_TaxID=4498;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. CDC Dancer;
PubMed=21784965; DOI=10.1104/pp.111.178822;
Meesapyodsuk D., Qiu X.;
"A peroxygenase pathway involved in the biosynthesis of epoxy Fatty
acids in oat.";
Plant Physiol. 157:454-463(2011).
[2]
PROTEIN SEQUENCE OF 10-35, FUNCTION, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=16956885; DOI=10.1074/jbc.M605395200;
Hanano A., Burcklen M., Flenet M., Ivancich A., Louwagie M., Garin J.,
Blee E.;
"Plant seed peroxygenase is an original heme-oxygenase with an EF-hand
calcium binding motif.";
J. Biol. Chem. 281:33140-33151(2006).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=14535881; DOI=10.1046/j.1365-313X.2003.01865.x;
Lequeu J., Fauconnier M.L., Chammai A., Bronner R., Blee E.;
"Formation of plant cuticle: evidence for the occurrence of the
peroxygenase pathway.";
Plant J. 36:155-164(2003).
-!- FUNCTION: Calcium-binding peroxygenase involved in cutin monomers
biosynthesis. Can catalyze epoxidation of fatty acid and
sulfoxidation reactions that can proceede competitively, although
in favor of the sulfoxidation. Can only use unsaturated fatty
acids with double bonds in the cis configuration as substrates.
The preferred substrate is oleic acid and is inactive toward
ricinoleic acid. Free fatty acid and fatty acid methyl esters are
effective substrate forms, but not phospholipids and acyl-CoA.
Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-
dienoic (HPODT) acids as oxygen donors.
{ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885,
ECO:0000269|PubMed:21784965}.
-!- CATALYTIC ACTIVITY: RH + ROOH = ROH + ROH.
{ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885,
ECO:0000269|PubMed:21784965}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.
{ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Inhibited by beta-mercaptoethanol and
organophosphorothioates such as parathion or terbufos.
{ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:21784965}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=16.07 uM for 9-HPOD {ECO:0000269|PubMed:21784965};
KM=10.42 uM for 9-HPOT {ECO:0000269|PubMed:21784965};
KM=25.18 uM for 13-HPOD {ECO:0000269|PubMed:21784965};
KM=7.25 uM for 13-HPOT {ECO:0000269|PubMed:21784965};
KM=215.76 uM for cumene hydroperoxide
{ECO:0000269|PubMed:21784965};
Vmax=214.04 pmol/sec/mg enzyme toward 9-HPOD
{ECO:0000269|PubMed:21784965};
Vmax=188.69 pmol/sec/mg enzyme toward 9-HPOT
{ECO:0000269|PubMed:21784965};
Vmax=306.57 pmol/sec/mg enzyme toward 13-HPOD
{ECO:0000269|PubMed:21784965};
Vmax=173.49 pmol/sec/mg enzyme toward 13-HPOT
{ECO:0000269|PubMed:21784965};
Vmax=883.34 pmol/sec/mg enzyme toward cumene hydroperoxide
{ECO:0000269|PubMed:21784965};
pH dependence:
Optimum pH is 7.0. {ECO:0000269|PubMed:21784965};
Temperature dependence:
Optimum temperature is 45 degrees Celsius.
{ECO:0000269|PubMed:21784965};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Microsome membrane. Lipid droplet.
-!- TISSUE SPECIFICITY: Expressed only in developing seeds. Not
detected in roots, leaves, glumes and germinating seeds.
{ECO:0000269|PubMed:21784965}.
-!- DOMAIN: Transmembrane regions are predicted by sequence analysis
tools, but these regions probably constitute hydrophobic domains
associated to phospholipids.
-!- DOMAIN: The proline-knot motif (124-133) may be involved in
targeting to lipid bodies.
-!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; JN390966; AEL03786.1; -; mRNA.
SMR; G1JSL4; -.
KEGG; ag:AEL03786; -.
KO; K17991; -.
BRENDA; 1.11.2.3; 588.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
InterPro; IPR007736; Caleosin-related.
PANTHER; PTHR31495; PTHR31495; 1.
Pfam; PF05042; Caleosin; 1.
1: Evidence at protein level;
Calcium; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
Lipid droplet; Membrane; Metal-binding; Microsome; Oxidoreductase.
CHAIN 1 249 Peroxygenase 1.
/FTId=PRO_0000415559.
DOMAIN 68 103 EF-hand.
CA_BIND 81 92 {ECO:0000255}.
MOTIF 124 133 Proline-knot.
METAL 76 76 Iron (heme axial ligand). {ECO:0000250}.
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


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