ID   PER38_ARATH             Reviewed;         346 AA.
AC   Q9LDA4;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 157.
DE   RecName: Full=Peroxidase 38;
DE            Short=Atperox P38;
DE            EC=1.11.1.7;
DE   Flags: Precursor;
GN   Name=PER38; Synonyms=P38; OrderedLocusNames=At4g08780;
GN   ORFNames=T32A17.90;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12034502; DOI=10.1016/s0378-1119(02)00465-1;
RA   Tognolli M., Penel C., Greppin H., Simon P.;
RT   "Analysis and expression of the class III peroxidase large gene family in
RT   Arabidopsis thaliana.";
RL   Gene 288:129-138(2002).
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.
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   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00297};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00297};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00297};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00297};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}.
CC       Note=C-terminal extension appears to target the protein to vacuoles.
CC   -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
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; AL161512; CAB78003.1; -; Genomic_DNA.
DR   EMBL; AL161813; CAB82114.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82677.1; -; Genomic_DNA.
DR   EMBL; OZ408686; CAO7046430.1; -; Genomic_DNA.
DR   PIR; C85088; C85088.
DR   RefSeq; NP_192618.1; NM_116948.2.
DR   AlphaFoldDB; Q9LDA4; -.
DR   SMR; Q9LDA4; -.
DR   FunCoup; Q9LDA4; 129.
DR   STRING; 3702.Q9LDA4; -.
DR   PeroxiBase; 204; AtPrx38.
DR   GlyCosmos; Q9LDA4; 2 sites, No reported glycans.
DR   GlyGen; Q9LDA4; 2 sites.
DR   MetOSite; Q9LDA4; -.
DR   PaxDb; 3702-Q9LDA4; -.
DR   ProteomicsDB; 236396; -.
DR   GeneID; 826448; -.
DR   KEGG; ath:AT4G08780; -.
DR   Araport; AT4G08780; -.
DR   TAIR; AT4G08780; -.
DR   eggNOG; ENOG502QVXS; Eukaryota.
DR   HOGENOM; CLU_010543_0_1_1; -.
DR   InParanoid; Q9LDA4; -.
DR   OMA; NESVSYM; -.
DR   PhylomeDB; Q9LDA4; -.
DR   BioCyc; ARA:AT4G08780-MONOMER; -.
DR   PRO; PR:Q9LDA4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9LDA4; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; ISM:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
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   FunFam; 1.10.420.10:FF:000001; Peroxidase; 1.
DR   FunFam; 1.10.520.10:FF:000001; 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; IPR019793; Peroxidases_heam-ligand_BS.
DR   InterPro; IPR033905; Secretory_peroxidase.
DR   PANTHER; PTHR31388:SF113; PEROXIDASE 37-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; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal; Vacuole.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..346
FT                   /note="Peroxidase 38"
FT                   /id="PRO_0000023704"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT                   ECO:0000255|PROSITE-ProRule:PRU10012"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         192
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   BINDING         193
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         247
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   BINDING         252
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   SITE            60
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q42578,
FT                   ECO:0000255|PROSITE-ProRule:PRU00297"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   DISULFID        66..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   DISULFID        119..323
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT   DISULFID        199..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ   SEQUENCE   346 AA;  38086 MW;  D5CD5762D9C03392 CRC64;
     MHSSLIKLGF LLLLLQVSLS HAQLSPSFYD KTCPQVFDIV TNTIVNALRS DPRIAASILR
     LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD VIDKMKAAIE KACPRTVSCA
     DMLAIAAKES IVLAGGPSWM VPNGRRDSLR GFMDLANDNL PGPSSTLKQL KDRFKNVGLD
     RSSDLVALSG GHTFGKSQCQ FIMDRLYNFG ETGLPDPTLD KSYLATLRKQ CPRNGNQSVL
     VDFDLRTPTL FDNKYYVNLK ENKGLIQSDQ ELFSSPDAAD TLPLVRAYAD GQGTFFDAFV
     KAIIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVDDAL EFASFM
//