ID A0A0Q3IGR2_BRADI Unreviewed; 439 AA.
AC A0A0Q3IGR2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940};
DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940};
GN Name=100836984 {ECO:0000313|EnsemblPlants:KQJ99867};
GN ORFNames=BRADI_3g45700v3 {ECO:0000313|EMBL:KQJ99867.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ99867.1};
RN [1] {ECO:0000313|EMBL:KQJ99867.1, ECO:0000313|EnsemblPlants:KQJ99867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99867.1,
RC ECO:0000313|EnsemblPlants:KQJ99867};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ99867.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99867.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ99867}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ99867};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate;
CC Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000939};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
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DR EMBL; CM000882; KQJ99867.1; -; Genomic_DNA.
DR RefSeq; XP_010235542.1; XM_010237240.2.
DR AlphaFoldDB; A0A0Q3IGR2; -.
DR EnsemblPlants; KQJ99867; KQJ99867; BRADI_3g45700v3.
DR GeneID; 100836984; -.
DR Gramene; KQJ99867; KQJ99867; BRADI_3g45700v3.
DR OrthoDB; 168803at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
DR ExpressionAtlas; A0A0Q3IGR2; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd00691; ascorbate_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR002207; Peroxidase_I.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356:SF67; L-ASCORBATE PEROXIDASE S, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 419..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..360
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 42..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 47333 MW; 9A33DF33ADA34911 CRC64;
MAERLASSAS LLPASPSPST RRAAAAAVAS FPSCSGSART GLRLRPSPSR FSQAAGRGRG
GAGGGLRVVR CMAASDAGQL KSAREDIKEI LKTNYCHPIL IRLGWHDSGT YDKNIEEWPL
RGGADGSLRF DPELSHGANA GLTSALKLIQ PIKDKYPGIT YADLFQLASA TAVEEAGGPK
IPMKYGRADI TSPEQCPPEG RLPDAGPRIP AEHLREVFYR MGLDDKEIVA LSGAHTLGRS
RPDRSGWGKS ETKYTKDGPG EPGGQSWTAE WLKFDNSYFK DIKEQRDQDL LVLPTDAALF
EDPSFKVYAE KYAEDQEAFF KDYAEAHAKL SNLGAKFDPP EGISLDDDKG DAPVEEKKVA
DADPAPADDN NGAASQPEPF VAAKYSYKKT ELSDTMKQKI RAEYEGLGGS PEKALQSNYF
LNIMIVIAGL AFLTSLLGS
//
