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Peroxidase 64 (Atperox P64) (EC 1.11.1.7) (ATP17a) (PRXR4)

 PER64_ARATH             Reviewed;         317 AA.
Q43872;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-JUL-2017, entry version 140.
RecName: Full=Peroxidase 64;
Short=Atperox P64;
EC=1.11.1.7;
AltName: Full=ATP17a;
AltName: Full=PRXR4;
Flags: Precursor;
Name=PER64; Synonyms=P64; OrderedLocusNames=At5g42180;
ORFNames=MJC20.29;
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 (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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).
[7]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=8425063; DOI=10.1007/BF00019954;
Trezzini G.F., Horrichs A., Somssich I.E.;
"Isolation of putative defense-related genes from Arabidopsis thaliana
and expression in fungal elicitor-treated cells.";
Plant Mol. Biol. 21:385-389(1993).
[8]
INDUCTION.
STRAIN=cv. Columbia;
PubMed=12172015; DOI=10.1105/tpc.003483;
Fowler S., Thomashow M.F.;
"Arabidopsis transcriptome profiling indicates that multiple
regulatory pathways are activated during cold acclimation in addition
to the CBF cold response pathway.";
Plant Cell 14:1675-1690(2002).
[9]
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.
-!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
radical of the donor + 2 H(2)O.
-!- 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:0000255|PROSITE-
ProRule:PRU00297}.
-!- TISSUE SPECIFICITY: Expressed in the whole plant, but
preferentially in roots.
-!- INDUCTION: Pathogen and elicitor-induced. Up-regulated transiently
by a cold treatment. {ECO:0000269|PubMed:12172015,
ECO:0000269|PubMed:8425063}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; X98316; CAA66960.1; -; mRNA.
EMBL; X99096; CAA67550.1; -; mRNA.
EMBL; AB017067; BAB08451.1; -; Genomic_DNA.
EMBL; CP002688; AED94776.1; -; Genomic_DNA.
EMBL; AY063962; AAL36318.1; -; mRNA.
EMBL; AY096403; AAM20043.1; -; mRNA.
RefSeq; NP_199033.1; NM_123583.4.
UniGene; At.23304; -.
ProteinModelPortal; Q43872; -.
SMR; Q43872; -.
STRING; 3702.AT5G42180.1; -.
PeroxiBase; 230; AtPrx64.
iPTMnet; Q43872; -.
PaxDb; Q43872; -.
PRIDE; Q43872; -.
EnsemblPlants; AT5G42180.1; AT5G42180.1; AT5G42180.
GeneID; 834223; -.
Gramene; AT5G42180.1; AT5G42180.1; AT5G42180.
KEGG; ath:AT5G42180; -.
Araport; AT5G42180; -.
TAIR; locus:2165820; AT5G42180.
eggNOG; ENOG410IHQ5; Eukaryota.
eggNOG; ENOG410YE7F; LUCA.
HOGENOM; HOG000237556; -.
InParanoid; Q43872; -.
KO; K00430; -.
OMA; MNDKTVP; -.
OrthoDB; EOG09360GIU; -.
PhylomeDB; Q43872; -.
BioCyc; ARA:AT5G42180-MONOMER; -.
PRO; PR:Q43872; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q43872; baseline and differential.
Genevisible; Q43872; AT.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0009664; P:plant-type cell wall organization; IBA:GO_Central.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
CDD; cd00693; secretory_peroxidase; 1.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR000823; Peroxidase_pln.
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; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; Heme;
Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 317 Peroxidase 64.
/FTId=PRO_0000023729.
ACT_SITE 63 63 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 64 64 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 67 67 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 69 69 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 71 71 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 73 73 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 188 188 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 189 189 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 241 241 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 243 243 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 248 248 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
BINDING 158 158 Substrate; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
SITE 59 59 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 111 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 65 70 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 117 313 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 195 227 {ECO:0000255|PROSITE-ProRule:PRU00297}.
SEQUENCE 317 AA; 34706 MW; 79536112BA918690 CRC64;
MNAHMLNLLV IVIFVVSFDV QALSPHYYDH TCPQADHIVT NAVKKAMSND QTVPAALLRM
HFHDCFVRGC DGSVLLDSKG KNKAEKDGPP NISLHAFYVI DNAKKALEEQ CPGIVSCADI
LSLAARDAVA LSGGPTWAVP KGRKDGRISK AIETRQLPAP TFNISQLRQN FGQRGLSMHD
LVALSGGHTL GFAHCSSFQN RLHKFNTQKE VDPTLNPSFA ARLEGVCPAH NTVKNAGSNM
DGTVTSFDNI YYKMLIQGKS LFSSDESLLA VPSTKKLVAK YANSNEEFER AFVKSMIKMS
SISGNGNEVR LNCRRVR


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