ID A0A2Z7AJV5_9LAMI Unreviewed; 274 AA.
AC A0A2Z7AJV5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=peroxidase {ECO:0000256|ARBA:ARBA00012313};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313};
GN ORFNames=F511_08802 {ECO:0000313|EMBL:KZV19461.1};
OS Dorcoceras hygrometricum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae;
OC Loxocarpinae; Dorcoceras.
OX NCBI_TaxID=472368 {ECO:0000313|EMBL:KZV19461.1, ECO:0000313|Proteomes:UP000250235};
RN [1] {ECO:0000313|EMBL:KZV19461.1, ECO:0000313|Proteomes:UP000250235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. XS01 {ECO:0000313|Proteomes:UP000250235};
RX PubMed=25902549; DOI=10.1073/pnas.1505811112;
RA Xiao L., Yang G., Zhang L., Yang X., Zhao S., Ji Z., Zhou Q., Hu M.,
RA Wang Y., Chen M., Xu Y., Jin H., Xiao X., Hu G., Bao F., Hu Y., Wan P.,
RA Li L., Deng X., Kuang T., Xiang C., Zhu J.K., Oliver M.J., He Y.;
RT "The resurrection genome of Boea hygrometrica: A blueprint for survival of
RT dehydration.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5833-5837(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000189};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the peroxidase family.
CC {ECO:0000256|RuleBase:RU004241}.
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DR EMBL; KV016696; KZV19461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z7AJV5; -.
DR OrthoDB; 1010072at2759; -.
DR Proteomes; UP000250235; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388:SF115; PEROXIDASE 4-RELATED; 1.
DR PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR600823-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KZV19461.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250235};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 1..272
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 7
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 13..18
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 66..268
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 274 AA; 29695 MW; D128AE8DD4416E38 CRC64;
MAASLIRLHF HDCFVQGCDA SILLDETPSI QSEKTAIPNI NSARGYNVIE DAKREVERLC
PRVVSCADIL TVAARDASVA VGGPSWNVKL GRKDSTTANR ARANSDLPSP FADANTLISA
FSVKGLTTRD MIALSGIYYI SSFTIAYTRP SPMLLFRSRI YSNGTDIDPG FASTRRRQCP
QTGGDSTLAP LDLVTPNSFD NNYFKNLVQR KGLLISDQVL FTSASTKDIV DGYSKNPRSF
AADFASAMIK MGEIQPLLAP NGIVRKTCGS ILVN
//
