PER1_SORBI
ID PER1_SORBI Reviewed; 362 AA.
AC P84516; C5XIP7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cationic peroxidase SPC4;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN OrderedLocusNames=Sb03g046810;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623;
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M.,
RA Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-213.
RC STRAIN=cv. RTx430 {ECO:0000269|Ref.2};
RA Cordonnier-Pratt M.-M., Wentzel V., Suzuki Y., Sugano S., Klein R.R.,
RA Liang C., Sun F., Sullivan R., Shah M., Rathore K., Eastman A., Pratt L.H.;
RT "An EST database from Sorghum: callus culture and cell suspension.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 32-58; 68-77 AND 127-164, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Cauga 105-15; TISSUE=Grain;
RX PubMed=16650004; DOI=10.1111/j.1742-4658.2006.05243.x;
RA Dicko M.H., Gruppen H., Hilhorst R., Voragen A.G.J., van Berkel W.J.H.;
RT "Biochemical characterization of the major sorghum grain peroxidase.";
RL FEBS J. 273:2293-2307(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 34-340 IN COMPLEX WITH CALCIUM;
RP HEME AND INDOLE-3-ACETATE, GLYCOSYLATION AT ASN-234 AND ASN-332, AND
RP DISULFIDE BONDS.
RX PubMed=26666777; DOI=10.1007/s00775-015-1313-z;
RA Nnamchi C.I., Parkin G., Efimov I., Basran J., Kwon H., Svistunenko D.A.,
RA Agirre J., Okolo B.N., Moneke A., Nwanguma B.C., Moody P.C., Raven E.L.;
RT "Structural and spectroscopic characterisation of a heme peroxidase from
RT sorghum.";
RL J. Biol. Inorg. Chem. 21:63-70(2016).
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 (By similarity). Has a high
CC preference for hydroxycinnamates as substrates. Substrate preference is
CC ferulic acid > p-coumaric acid > N-acetyl tyrosine methyl ester > N-
CC acetyl-tyrosine > tyrosine > catechol > Gly-Tyr-Gly. May be involved in
CC the formation of diferulate linkages in the plant cell wall
CC (PubMed:16650004). {ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:16650004}.
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:0000269|PubMed:16650004};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:16650004, ECO:0000269|PubMed:26666777};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:16650004,
CC ECO:0000269|PubMed:26666777};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:16650004, ECO:0000269|PubMed:26666777};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297, ECO:0000269|PubMed:16650004,
CC ECO:0000269|PubMed:26666777};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.8 with 2.2'-azino-bis(3-ethylbenzthiazoline-6-
CC sulfonic acid) as substrate, 5.5 with ferulic acid as substrate, and
CC 6.5 with N-acetyl-L-tyrosine as substrate.;
CC Temperature dependence:
CC Loss of activity at temperature above 55 degrees Celsius. In the
CC presence of excess calcium, full activity is kept at 65 degrees
CC Celsius for 90 minutes.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16650004}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:16650004}.
CC -!- TISSUE SPECIFICITY: Present in germinated and ungerminated grain,
CC seedlings, and leaves and stem of the mature plant.
CC {ECO:0000269|PubMed:16650004}.
CC -!- PTM: The proportions of glycoforms I and II are 35% and 65%
CC respectively.
CC -!- MASS SPECTROMETRY: Mass=33246; Mass_error=50; Method=MALDI;
CC Note=Deglycosylated form.; Evidence={ECO:0000269|PubMed:16650004};
CC -!- MASS SPECTROMETRY: Mass=34283; Mass_error=50; Method=MALDI;
CC Note=Glycoform I.; Evidence={ECO:0000269|PubMed:16650004};
CC -!- MASS SPECTROMETRY: Mass=35631; Mass_error=50; Method=MALDI;
CC Note=Glycoform II.; Evidence={ECO:0000269|PubMed:16650004};
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; CM000762; EES02106.1; -; Genomic_DNA.
DR EMBL; CD222694; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CD226279; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_002456986.1; XM_002456941.1.
DR PDB; 5AOG; X-ray; 1.27 A; A=34-340.
DR PDBsum; 5AOG; -.
DR AlphaFoldDB; P84516; -.
DR SMR; P84516; -.
DR STRING; 4558.Sb03g046810.1; -.
DR PeroxiBase; 853; SbPrx69.
DR PRIDE; P84516; -.
DR EnsemblPlants; EES02106; EES02106; SORBI_3003G437400.
DR GeneID; 8074114; -.
DR Gramene; EES02106; EES02106; SORBI_3003G437400.
DR KEGG; sbi:8074114; -.
DR eggNOG; ENOG502QT8W; Eukaryota.
DR HOGENOM; CLU_010543_0_0_1; -.
DR InParanoid; P84516; -.
DR OMA; TVAMIKM; -.
DR OrthoDB; 948884at2759; -.
DR BRENDA; 1.11.1.7; 5768.
DR Proteomes; UP000000768; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235; PTHR31235; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:16650004"
FT CHAIN 32..362
FT /note="Cationic peroxidase SPC4"
FT /id="PRO_0000045853"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P22195,
FT ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-
FT ProRule:PRU10012"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 111
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT /evidence="ECO:0000269|PubMed:26666777,
FT ECO:0007744|PDB:5AOG"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 211
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26666777,
FT ECO:0007744|PDB:5AOG"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT SITE 77
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P22195,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26666777,
FT ECO:0007744|PDB:5AOG"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26666777,
FT ECO:0007744|PDB:5AOG"
FT DISULFID 50..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT DISULFID 83..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT DISULFID 138..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT DISULFID 218..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:26666777, ECO:0007744|PDB:5AOG"
FT TURN 43..49
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:5AOG"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:5AOG"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:5AOG"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5AOG"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:5AOG"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5AOG"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:5AOG"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:5AOG"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:5AOG"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:5AOG"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5AOG"
SQ SEQUENCE 362 AA; 38452 MW; 13AB5B89D77CC6E5 CRC64;
MSRAPTLAAA AAVAAVVLIC SSSTATAADG NARQPPLAPG LSFDFYKRSC PKAESIVRSF
VQDAVRRDVG LAAGLLRLHF HDCFVQGCDA SVLLDGSATG PGEQQAPPNL TLRPTAFKAI
NDIHDRLHKE CGGTVVSCSD VLALAARDSV VVSGGPSYKV PLGRRDSASF ATQQDVLSGL
PPPTAAVPAL LAVLSKINLD ATDLVALSGG HTIGLGHCTS FEDRLFPRPD PTLNATFAGQ
LRRTCPAKGT DRRTPLDVRT PNAFDNKYYV NLVNREGLFT SDQDLFSNAR TRALVDKFAR
SQRDFFDQFA FSVVKMGQIK VLTGTQGQIR TNCSARNAAG TTMLPWSVSV VEEAADESLG
VF
