ID PER68_ARATH Reviewed; 325 AA.
AC Q9LVL1;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 30-NOV-2016, entry version 118.
DE RecName: Full=Peroxidase 68;
DE Short=Atperox P68;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN Name=PER68; Synonyms=P68; OrderedLocusNames=At5g58400;
GN ORFNames=MCK7.27;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA Shibata K., Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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
RT in 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
CC catabolism, response to environmental stresses such as wounding,
CC pathogen attack and oxidative stress. These functions might be
CC dependent on each isozyme/isoform in each plant tissue.
CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
CC radical of the donor + 2 H(2)O.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC subunit. {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-
CC ProRule:PRU00297}.
CC -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant
CC (class III) peroxidase subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00297}.
DR EMBL; AB019228; BAA96931.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97048.1; -; Genomic_DNA.
DR EMBL; AK118274; BAC42892.1; -; mRNA.
DR EMBL; BT008527; AAP40354.1; -; mRNA.
DR RefSeq; NP_200648.1; NM_125226.4.
DR UniGene; At.29282; -.
DR ProteinModelPortal; Q9LVL1; -.
DR SMR; Q9LVL1; -.
DR STRING; 3702.AT5G58400.1; -.
DR PeroxiBase; 234; AtPrx68.
DR PaxDb; Q9LVL1; -.
DR PRIDE; Q9LVL1; -.
DR EnsemblPlants; AT5G58400.1; AT5G58400.1; AT5G58400.
DR GeneID; 835953; -.
DR Gramene; AT5G58400.1; AT5G58400.1; AT5G58400.
DR KEGG; ath:AT5G58400; -.
DR TAIR; AT5G58400; -.
DR HOGENOM; HOG000237557; -.
DR InParanoid; Q9LVL1; -.
DR KO; K00430; -.
DR OMA; MECYEQS; -.
DR OrthoDB; EOG09360G9Q; -.
DR PhylomeDB; Q9LVL1; -.
DR BioCyc; ARA:AT5G58400-MONOMER; -.
DR PRO; PR:Q9LVL1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR Genevisible; Q9LVL1; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR010255; Haem_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
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 2: Evidence at transcript level;
KW Calcium; Complete proteome; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1 28 {ECO:0000255}.
FT CHAIN 29 325 Peroxidase 68.
FT /FTId=PRO_0000023733.
FT ACT_SITE 70 70 Proton acceptor. {ECO:0000255|PROSITE-
FT ProRule:PRU00297, ECO:0000255|PROSITE-
FT ProRule:PRU10012}.
FT METAL 71 71 Calcium 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT METAL 74 74 Calcium 1; via carbonyl oxygen.
FT {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT METAL 76 76 Calcium 1; via carbonyl oxygen.
FT {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT METAL 78 78 Calcium 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT METAL 80 80 Calcium 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT METAL 198 198 Iron (heme axial ligand).
FT {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT METAL 199 199 Calcium 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT METAL 245 245 Calcium 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT METAL 248 248 Calcium 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT METAL 253 253 Calcium 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00297}.
FT BINDING 168 168 Substrate; via carbonyl oxygen.
FT {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT SITE 66 66 Transition state stabilizer.
FT {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT MOD_RES 29 29 Pyrrolidone carboxylic acid.
FT {ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297}.
FT CARBOHYD 99 99 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 214 214 N-linked (GlcNAc...). {ECO:0000255}.
FT DISULFID 39 119 {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT DISULFID 72 77 {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT DISULFID 125 321 {ECO:0000255|PROSITE-ProRule:PRU00297}.
FT DISULFID 205 230 {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 190 200 ipat:PEROXIDASE_1 [T]
FT MYHIT 46 289 ipfam:peroxidase [T]
FT MYHIT 29 325 iprf:PEROXIDASE_4 [T]
FT MYHIT 61 72 ipat:PEROXIDASE_2 [T]
SQ SEQUENCE 325 AA; 35627 MW; 52CD84C9D11019B5 CRC64;
MECYEQSRQR AAFVVLLFIV MLGSQAQAQL RTDFYSDSCP SLLPTVRRVV QREVAKERRI
AASLLRLFFH DCFVNGCDAS ILLDDTRSFL GEKTAGPNNN SVRGYEVIDA IKSRVERLCP
GVVSCADILA ITARDSVLLM GGRGWSVKLG RRDSITASFS TANSGVLPPP TSTLDNLINL
FRANGLSPRD MVALSGAHTI GQARCVTFRS RIYNSTNIDL SFALSRRRSC PAATGSGDNN
AAILDLRTPE KFDGSYFMQL VNHRGLLTSD QVLFNGGSTD SIVVSYSRSV QAFYRDFVAA
MIKMGDISPL TGSNGQIRRS CRRPN
//
|
