PXG_ORYSI
ID PXG_ORYSI Reviewed; 244 AA.
AC A2XVG1; Q40679;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Peroxygenase;
DE EC=1.11.2.3;
GN Name=PXG; Synonyms=EFA27; ORFNames=OsI_16610;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. IR36;
RX PubMed=8550584; DOI=10.1074/jbc.271.1.343;
RA Frandsen G., Muller-Uri F., Nielsen M., Mundy J., Skriver K.;
RT "Novel plant Ca(2+)-binding protein expressed in response to abscisic acid
RT and osmotic stress.";
RL J. Biol. Chem. 271:343-348(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [4]
RP CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Calcium-binding peroxygenase involved in the degradation of
CC storage lipid in oil bodies. May be involved in the interaction between
CC oil bodies and vacuoles during seed germination and in the oxylipin
CC signaling pathways and plant defense responses. Can catalyze
CC sulfoxidation of thiobenzamide, hydroxylation of aniline and
CC epoxidation of oleic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
CC Evidence={ECO:0000269|PubMed:16956885};
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:8550584}.
CC Lipid droplet {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in developing seeds and in osmotically
CC stressed vegetative tissues. Not detected in shoots under normal growth
CC conditions. {ECO:0000269|PubMed:8550584}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late embryogenesis in embryos but
CC not in endosperm. {ECO:0000269|PubMed:8550584}.
CC -!- INDUCTION: Up-regulated by abscisic acid and osmotic stresses.
CC {ECO:0000269|PubMed:8550584}.
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 (120-129) may be involved in targeting
CC to lipid bodies.
CC -!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
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DR EMBL; X89891; CAA61981.1; -; mRNA.
DR EMBL; CR855236; CAH68004.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY94821.1; -; Genomic_DNA.
DR PIR; T03731; T03731.
DR AlphaFoldDB; A2XVG1; -.
DR STRING; 39946.A2XVG1; -.
DR EnsemblPlants; BGIOSGA014735-TA; BGIOSGA014735-PA; BGIOSGA014735.
DR Gramene; BGIOSGA014735-TA; BGIOSGA014735-PA; BGIOSGA014735.
DR HOGENOM; CLU_062049_0_1_1; -.
DR OMA; GWIIAKG; -.
DR Proteomes; UP000007015; Chromosome 4.
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; Endoplasmic reticulum; Heme; Iron; Lipid droplet; Membrane;
KW Metal-binding; Microsome; Oxidoreductase; Reference proteome.
FT CHAIN 1..244
FT /note="Peroxygenase"
FT /id="PRO_0000415562"
FT DOMAIN 64..99
FT /note="EF-hand"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..129
FT /note="Proline-knot"
FT BINDING 72
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 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
SQ SEQUENCE 244 AA; 27414 MW; DE1DF19133D700D5 CRC64;
MAEEAASKAA PTDALSSVAA EAPVTRERPV RADLEVQIPK PYLARALVAP DVYHPEGTEG
RDHRQMSVLQ QHVAFFDLDG DGIVYPWETY GGLRELGFNV IVSFFLAIAI NVGLSYPTLP
SWIPSLLFPI HIKNIHRAKH GSDSSTYDNE GRFMPVNFES IFSKNARTAP DKLTFGDIWR
MTEGQRVALD LLGRIASKGE WILLYVLAKD EEGFLRKEAV RRCFDGSLFE SIAQQRREAH
EKQK
