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Peroxidase 32 (Atperox P32) (EC 1.11.1.7) (ATP16a) (PRXR3)

 PER32_ARATH             Reviewed;         352 AA.
Q9LHB9; Q43732; Q6K1J2;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 3.
16-JAN-2019, entry version 134.
RecName: Full=Peroxidase 32;
Short=Atperox P32;
EC=1.11.1.7;
AltName: Full=ATP16a;
AltName: Full=PRXR3;
Flags: Precursor;
Name=PER32; Synonyms=P32; OrderedLocusNames=At3g32980;
ORFNames=T15D2.7, T15D2.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H.,
Simon P.;
"Eleven cDNA clones from Arabidopsis thaliana encoding
isoperoxidases.";
(er) Plant Gene Register PGR96-066(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F.,
Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N.,
Rasmussen S.K.;
"From expressed sequence tags to structure, function, evolution and
expression of 28 ER-targeted Arabidopsis peroxidases.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Tognolli M., Greppin H., Simon P.;
"Structure of the gene encoding Arabidopsis thaliana PRXR3
peroxidase.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Nakamura Y.;
"Structural analysis of Arabidopsis thaliana chromosome 3. III.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
CHARACTERIZATION.
STRAIN=cv. Columbia;
PubMed=9738941; DOI=10.1016/S0014-5793(98)00849-7;
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S.,
Welinder K.G.;
"Computational analyses and annotations of the Arabidopsis peroxidase
gene family.";
FEBS Lett. 433:98-102(1998).
[9]
CHARACTERIZATION.
STRAIN=cv. Columbia;
Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M.,
Simon P., Penel C.;
"Identification and characterization of Ca(2+)-pectate binding
peroxidases in Arabidopsis thaliana.";
J. Plant Physiol. 159:1165-1171(2002).
[10]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=9807821; DOI=10.1046/j.1365-313X.1998.00254.x;
Ruan Y., Gilmore J., Conner T.;
"Towards Arabidopsis genome analysis: monitoring expression profiles
of 1400 genes using cDNA microarrays.";
Plant J. 15:821-833(1998).
[11]
TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X.;
"Toward elucidating the global gene expression patterns of developing
Arabidopsis: parallel analysis of 8300 genes by a high-density
oligonucleotide probe array.";
Plant Physiol. Biochem. 39:221-242(2001).
[12]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=11748215; DOI=10.1074/jbc.M104863200;
Scheideler M., Schlaich N.L., Fellenberg K., Beissbarth T.,
Hauser N.C., Vingron M., Slusarenko A.J., Hoheisel J.D.;
"Monitoring the switch from housekeeping to pathogen defense
metabolism in Arabidopsis thaliana using cDNA arrays.";
J. Biol. Chem. 277:10555-10561(2002).
[13]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=12034502; DOI=10.1016/S0378-1119(02)00465-1;
Tognolli M., Penel C., Greppin H., Simon P.;
"Analysis and expression of the class III peroxidase large gene family
in Arabidopsis thaliana.";
Gene 288:129-138(2002).
-!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
biosynthesis and degradation of lignin, suberization, auxin
catabolism, response to environmental stresses such as wounding,
pathogen attack and oxidative stress. These functions might be
dependent on each isozyme/isoform in each plant tissue.
-!- FUNCTION: Exhibits a Ca(2+)-pectate binding affinity which could
be interpreted in vivo as a specificity to interact with the
pectic structure of the cell wall.
-!- CATALYTIC ACTIVITY:
Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor +
2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377,
ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521;
EC=1.11.1.7;
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000255|PROSITE-ProRule:PRU00297};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00297};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole
{ECO:0000305}. Note=Carboxy-terminal extension appears to target
the protein to vacuoles.
-!- TISSUE SPECIFICITY: Strongly expressed in roots.
{ECO:0000269|PubMed:9807821, ECO:0000269|Ref.11}.
-!- INDUCTION: Late induced by infection with an incompatible
bacterial plant pathogen. {ECO:0000269|PubMed:11748215}.
-!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
-!- SIMILARITY: Belongs to the peroxidase family. Classical plant
(class III) peroxidase subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X98315; CAA66959.1; -; mRNA.
EMBL; X98777; CAA67313.1; -; mRNA.
EMBL; AJ133036; CAB37193.1; -; Genomic_DNA.
EMBL; AP002054; BAB02631.1; -; Genomic_DNA.
EMBL; CP002686; AEE77707.1; -; Genomic_DNA.
EMBL; AY080608; AAL86292.1; -; mRNA.
EMBL; AY133730; AAM91664.1; -; mRNA.
EMBL; AY087285; AAM64838.1; -; mRNA.
RefSeq; NP_850652.1; NM_180321.4.
UniGene; At.47588; -.
UniGene; At.67710; -.
UniGene; At.71576; -.
ProteinModelPortal; Q9LHB9; -.
SMR; Q9LHB9; -.
BioGrid; 8393; 1.
IntAct; Q9LHB9; 1.
STRING; 3702.AT3G32980.1; -.
PeroxiBase; 198; AtPrx32.
PaxDb; Q9LHB9; -.
PRIDE; Q9LHB9; -.
EnsemblPlants; AT3G32980.1; AT3G32980.1; AT3G32980.
GeneID; 823067; -.
Gramene; AT3G32980.1; AT3G32980.1; AT3G32980.
KEGG; ath:AT3G32980; -.
Araport; AT3G32980; -.
TAIR; locus:2097273; AT3G32980.
eggNOG; ENOG410JAWC; Eukaryota.
eggNOG; ENOG41119N5; LUCA.
HOGENOM; HOG000237557; -.
InParanoid; Q9LHB9; -.
KO; K00430; -.
OMA; YTNIEAR; -.
OrthoDB; 819626at2759; -.
PhylomeDB; Q9LHB9; -.
BioCyc; ARA:AT3G32980-MONOMER; -.
PRO; PR:Q9LHB9; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LHB9; baseline and differential.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
CDD; cd00693; secretory_peroxidase; 1.
InterPro; IPR002016; Haem_peroxidase.
InterPro; IPR010255; Haem_peroxidase_sf.
InterPro; IPR000823; Peroxidase_pln.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
InterPro; IPR033905; Secretory_peroxidase.
Pfam; PF00141; peroxidase; 1.
PRINTS; PR00458; PEROXIDASE.
PRINTS; PR00461; PLPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; Heme;
Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
Vacuole.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 352 Peroxidase 32.
/FTId=PRO_0000023698.
ACT_SITE 71 71 Proton acceptor.
METAL 72 72 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 75 75 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 77 77 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 79 79 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 81 81 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 199 199 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 200 200 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 251 251 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 254 254 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 259 259 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
BINDING 168 168 Substrate; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
SITE 67 67 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
MOD_RES 30 30 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:Q42578,
ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 120 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 73 78 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 126 330 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 206 238 {ECO:0000255|PROSITE-ProRule:PRU00297}.
CONFLICT 24 24 S -> L (in Ref. 1, 2, 3 and 7).
{ECO:0000305}.
CONFLICT 145 145 S -> Y (in Ref. 7; AAM64838).
{ECO:0000305}.
SEQUENCE 352 AA; 38847 MW; 765696B3869BA1DB CRC64;
MNFSYSSLST WTTLMTLGCL LLHSSISSAQ LTPTFYDNTC PSVFTIVRDT IVNELRSDPR
IAASILRLHF HDCFVNGCDA SILLDNTTSF RTEKDAAPNA NSARGFPVID RMKAAVETAC
PRTVSCADIL TIAAQQAVNL AGGPSWRVPL GRRDSLQAFF ALANTNLPAP FFTLPQLKAS
FQNVGLDRPS DLVALSGGHT FGKNQCQFIM DRLYNFSNTG LPDPTLNTTY LQTLRGQCPR
NGNQTVLVDF DLRTPTVFDN KYYVNLKELK GLIQTDQELF SSPNATDTIP LVREYADGTQ
KFFNAFVEAM NRMGNITPLT GTQGQIRQNC RVVNSNSLLH DVVEIVDFVS SM


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