ID A0A2P5WBV7_GOSBA Unreviewed; 361 AA.
AC A0A2P5WBV7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=Peroxidase {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060};
DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060};
GN ORFNames=GOBAR_AA32133 {ECO:0000313|EMBL:PPR88557.1};
OS Gossypium barbadense (Sea-island cotton) (Egyptian cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3634 {ECO:0000313|EMBL:PPR88557.1, ECO:0000313|Proteomes:UP000239757};
RN [1] {ECO:0000313|EMBL:PPR88557.1, ECO:0000313|Proteomes:UP000239757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Xinhai21 {ECO:0000313|Proteomes:UP000239757};
RC TISSUE=Leaf {ECO:0000313|EMBL:PPR88557.1};
RA Chen X., Liu X., Zhao B., Zheng H., Hu Y., Lu G., Yang C., Chen J.,
RA Shan C., Zhang L., Zhou Y., Wang L., Guo W., Bai Y., Ruan J., Shangguan X.,
RA Mao Y., Jiang J., Zhu Y., Lei J., Kang H., Chen S., He X., Wang R.,
RA Wang Y., Chen J., Wang L., Yu S., Wang B., Wei J., Song S., Lu X., Gao Z.,
RA Gu W., Deng X., Ma D., Wang S., Liang W., Fang L., Cai C., Zhu X., Zhou B.,
RA Zhang Y., Chen Z., Xu S., Zhu R., Wang S., Zhang T., Zhao G.;
RT "Genome of allotetraploid Gossypium barbadense reveals genomic plasticity
RT and fiber elongation in cotton evolution.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue. {ECO:0000256|ARBA:ARBA00002322}.
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 ECO:0000256|RuleBase:RU362060};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC ECO:0000256|RuleBase:RU362060};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC 3, ECO:0000256|RuleBase:RU362060};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU362060};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|RuleBase:RU362060};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}.
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DR EMBL; KZ668238; PPR88557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5WBV7; -.
DR Proteomes; UP000239757; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR CDD; cd00693; secretory_peroxidase; 1.
DR Gene3D; 1.10.520.10; -; 2.
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; PTHR31235:SF368; PEROXIDASE 25; 1.
DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1.
DR Pfam; PF00141; peroxidase; 2.
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, ECO:0000256|RuleBase:RU362060};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR600823-5};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362060};
KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362060};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR600823-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362060};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060};
KW Reference proteome {ECO:0000313|Proteomes:UP000239757};
KW Secreted {ECO:0000256|RuleBase:RU362060}.
FT DOMAIN 112..360
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT SITE 149
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT DISULFID 122..198
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 155..160
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT DISULFID 204..356
FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ SEQUENCE 361 AA; 39287 MW; E6775623E7D08F69 CRC64;
MAAWDEICVK DLFSTSGDSW DEGLVKSLLA LRMFVGDNWV VLARGSLKCN IDAAMSSPHG
LGESHMAELL AVREALSWLR EEGYDNVEPE ADCSGPVYVF SKNKYANGQG SGLQNGFYSS
SCPKAEAVVR STVESHFNKD PTIAAALLRL HFHDCFVQGC DGSVLISGSS AERSALPNLG
LRGFEVIDDA KAQLESLCPG IVSCADLLAL AARDTVDLVT FLRPHTVMVQ VGLFQPEEGM
AGGTYHRTNG LLVLPVPPIQ LHNNRNDGSK KVGLDIGSET KFDVSFFKNV RDGKGVLESD
QRLWGDDGTR RVVENYAGNV RGLLGLRFDY EFRKAMIKMS SIEVKTGSDG EIRKTCSKIN
T
//
