Q0D8I7 · Q0D8I7_ORYSJ
- ProteinOs07g0157000 protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1461 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 58 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 62 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 63 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 68 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 70 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 72 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 85 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 156 | substrate | ||||
Sequence: P | ||||||
Binding site | 186 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metal ion transmembrane transporter activity | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ0D8I7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 323-341 | Helical | ||||
Sequence: LITGICFATVVPNLLPYAI | ||||||
Transmembrane | 348-370 | Helical | ||||
Sequence: MVGTLNACIAGFALLCYVLGLLV | ||||||
Transmembrane | 390-409 | Helical | ||||
Sequence: SAYSLMALLGANVMAHNFYI | ||||||
Transmembrane | 421-445 | Helical | ||||
Sequence: AFAVGALFHDHLFSVLFIFTGIFLV | ||||||
Transmembrane | 480-502 | Helical | ||||
Sequence: MAPTIFLVVLLFSSHIISLTSAI | ||||||
Transmembrane | 546-568 | Helical | ||||
Sequence: YQLLIICQIIQAMLLPSSVVPLF | ||||||
Transmembrane | 588-609 | Helical | ||||
Sequence: ILTFLAFLLMLFSNIIFMAEML | ||||||
Transmembrane | 629-650 | Helical | ||||
Sequence: FPSTVLITVACVSVAFSLYMAV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKLILMVAFQAMSLISISTA | ||||||
Chain | PRO_5004170990 | 21-1461 | ||||
Sequence: SLQYNFYGSSCPNAEQTISNVVYGLIDADPSMAPALLRLHFHDCFVMGCDASILLDPTKANGSPEKTAIPLRGYDAVNKIKAAVEAVCPGKVSCADILAFAARDSVAKSGGFVYPVPAGSRDGNVSSAFSVFSSIPSPFFDAGELVQSFAAKGLTVDDLVALSGAHSIGTAHCSGFKNRLYPTVDASLDASYAAALRAACPDGSAADDGVVNNSPVSPATLGNQYFKNALAGRVLFTSDAALLTGQNDTAEKVRENAGDLTAWMARFAASMVKMGGIEVLTGARGEIFGIALGFNLLFEYDDLITGICFATVVPNLLPYAISHLGKKMVGTLNACIAGFALLCYVLGLLVSQPQIPLTTNVIFPKLSGESAYSLMALLGANVMAHNFYIHSSVVQGQKRSAFAVGALFHDHLFSVLFIFTGIFLVNHVLMNSAAADSTNTLLLTFQDVVELMNQIFVNPMAPTIFLVVLLFSSHIISLTSAIGSQVISQHLFGINLPLSGHHLILKAFAIVPALYCAKVAGAEGIYQLLIICQIIQAMLLPSSVVPLFRVASSRLIMGAHRVSLHLEILTFLAFLLMLFSNIIFMAEMLFGDSGWLNTLKGNTGSPVVFPSTVLITVACVSVAFSLYMAVTPLKSGSHEAELQQEWSVPSQKELLNTTQDREETCAGNVTYEEDQRSDVVPSPRIQPVDCLKSALDYIDSSDTAIESDHDSQHSTAHTSTAPESCHSPSFIPEESKSVVAVDWPEPLEPISNAIVAEESTVESVDSKSTGERDIEVEPALLMDNDKEAPNILESDNKSLGGNNPSCASDDGPPSLTFSRGKGSDAGNGSGSLSRLSGLGRAARRQLAAILDEFWGHLFDYHGKLTQEASSKRFDILLGLDVRTPSSTVRADSQANEIPKSPMVRDNLQGSAFLGSSRDLMSTKNEMSNLDLTYGLQMGNNIGSSAWSQGMQLPSTQLQSSSNSLLDQGARLNSNFSTPSYADNNQFYQPATIHGYQLASYLKQMNANRNPYSSMPLDPQRLPKSSASAVPTYVDSVMHARNQNLLASLGATPSQIAATSRIERSYYVPSTLDGNENAGSSAYSKKYHSSPDISALIAASRSALLNESKLGGGTIGSQSYLSRLASERSQYTNSVARPAAPLAFDELSPPKLPGDIFSMQQSPNPSARSLWAKQPFEQLFGVSSAELTKSEFNPAGRSGGMTKDDFSYKESEAKLLQSLRFCISKLLKLEGSGWLFKQNGGSDEDLIDQVAAVEKLLQQGTSDNQLLLGDTQQPPCDKADIQYMRVLPNCGDDCIWRASLVVSFGVWCIRRVLDLSLVESRPELWGKYTYVLNRLQGILDPAFSKPRSALSACACLHRDIRVLNSLRHSSLVATNSIPRQIRGSFTTASVVLEMIKDVETAVSGRKGRSGTAAGDVAFPKGKENLASVLKRYKRRLSSKGQQ | ||||||
Disulfide bond | 31↔108 | |||||
Sequence: CPNAEQTISNVVYGLIDADPSMAPALLRLHFHDCFVMGCDASILLDPTKANGSPEKTAIPLRGYDAVNKIKAAVEAVC | ||||||
Disulfide bond | 64↔69 | |||||
Sequence: CFVMGC | ||||||
Disulfide bond | 193↔220 | |||||
Sequence: CSGFKNRLYPTVDASLDASYAAALRAAC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-315 | Plant heme peroxidase family profile | ||||
Sequence: SLQYNFYGSSCPNAEQTISNVVYGLIDADPSMAPALLRLHFHDCFVMGCDASILLDPTKANGSPEKTAIPLRGYDAVNKIKAAVEAVCPGKVSCADILAFAARDSVAKSGGFVYPVPAGSRDGNVSSAFSVFSSIPSPFFDAGELVQSFAAKGLTVDDLVALSGAHSIGTAHCSGFKNRLYPTVDASLDASYAAALRAACPDGSAADDGVVNNSPVSPATLGNQYFKNALAGRVLFTSDAALLTGQNDTAEKVRENAGDLTAWMARFAASMVKMGGIEVLTGARGEIFGIALGFN | ||||||
Region | 725-750 | Disordered | ||||
Sequence: IESDHDSQHSTAHTSTAPESCHSPSF | ||||||
Region | 778-850 | Disordered | ||||
Sequence: ESTVESVDSKSTGERDIEVEPALLMDNDKEAPNILESDNKSLGGNNPSCASDDGPPSLTFSRGKGSDAGNGSG | ||||||
Compositional bias | 784-812 | Basic and acidic residues | ||||
Sequence: VDSKSTGERDIEVEPALLMDNDKEAPNIL | ||||||
Compositional bias | 815-832 | Polar residues | ||||
Sequence: DNKSLGGNNPSCASDDGP |
Sequence similarities
Belongs to the NRAMP (TC 2.A.55) family.
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,461
- Mass (Da)156,868
- Last updated2006-10-17 v1
- Checksum10749D05CFD7AF5C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 784-812 | Basic and acidic residues | ||||
Sequence: VDSKSTGERDIEVEPALLMDNDKEAPNIL | ||||||
Compositional bias | 815-832 | Polar residues | ||||
Sequence: DNKSLGGNNPSCASDDGP |