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UniProtKB/Swiss-Prot entry Q39034


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PER59_ARATH
Primary accession number Q39034
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on December 6, 2002 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 77)
Name and origin of the protein
Protein name Peroxidase 59 [Precursor]
Synonyms Atperox P59
EC 1.11.1.7
Peroxidase N
ATPN
Gene name
Name: PER59
Synonyms: P59
OrderedLocusNames: At5g19890
ORFNames: F28I16.40
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Oestergaard L., Welinder K.G.;
"Sequence analysis and expression of two peroxidase encoding mRNAs from Arabidopsis thaliana.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
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.
[5]
CHARACTERIZATION.
STRAIN=cv. Columbia;
DOI=10.1016/S0014-5793(98)00849-7; PubMed=9738941 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME, AND DISULFIDE BONDS.
STRAIN=cv. Columbia;
DOI=10.1107/S0907444999016340; PubMed=10713531 [NCBI, ExPASy, EBI, Israel, Japan]
Mirza O., Henriksen A., Oestergaard L., Welinder K.G., Gajhede M.;
"Arabidopsis thaliana peroxidase N: structure of a novel neutral peroxidase.";
Acta Crystallogr. D 56:372-375(2000).
[7]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
DOI=10.1016/S0378-1119(02)00465-1; PubMed=12034502 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X98453; CAA67092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AY123985; AAM74498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000582; AAN18151.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY088025; AAM65571.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_568385.1; -.
UniGene At.143
3D structure databases
PDB
1QGJ; X-ray; 1.90 A; A/B=29-328.[ExPASy / RCSB / EBI]
PDBsum 1QGJ; -.
ModBase Q39034.
Protein family/group databases
PeroxiBase 225; AtPrx59.
Organism-specific databases
GeneFarm 1914; 61.
TAIR At5g19890; -.
Gene expression databases
ArrayExpress Q39034; -.
GermOnline AT5G19890; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000823; Peroxidase_pln.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00458; PEROXIDASE.
PR00461; PLPEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q39034.
Genome annotation databases
GeneID 832111; -.
GenomeReviews BA000015_GR; AT5G19890.
KEGG ath:AT5G19890; -.
NMPDR fig|3702.1.peg.24192; -.
Other
DrugBank DB00143; Glutathione.
ProtoNet Q39034.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     Potential. 
CHAIN   29   328  300     Peroxidase 59. PRO_0000023724
ACT_SITE   70    70        Proton acceptor. 
METAL   71    71        Calcium 1. 
METAL   74    74        Calcium 1; via carbonyl oxygen. 
METAL   76    76        Calcium 1; via carbonyl oxygen. 
METAL   78    78        Calcium 1. 
METAL   80    80        Calcium 1. 
METAL   193   193        Iron (heme axial ligand). 
METAL   194   194        Calcium 2. 
METAL   245   245        Calcium 2. 
METAL   248   248        Calcium 2. 
METAL   251   251        Calcium 2; via carbonyl oxygen. 
METAL   253   253        Calcium 2. 
BINDING   163   163        Substrate; via carbonyl oxygen. 
SITE   66    66  1     Transition state stabilizer. 
MOD_RES   29    29        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   182   182        N-linked (GlcNAc...) (Potential). 
CARBOHYD   209   209        N-linked (GlcNAc...) (Potential). 
CARBOHYD   239   239        N-linked (GlcNAc...) (Potential). 
CARBOHYD   281   281        N-linked (GlcNAc...) (Potential). 
CARBOHYD   310   310        N-linked (GlcNAc...) (Potential). 
DISULFID   39   116         
DISULFID   72    77         
DISULFID   122   323         
DISULFID   200   232         
CONFLICT   3     3        T -> R (in Ref. 4; AAM65571). 
CONFLICT   213   213        L -> A (in Ref. 1 and 4). 
TURN   32    38  7      
HELIX   42    56  15      
HELIX   60    72  13      
TURN   73    75  3      
STRAND   76    79  4      
HELIX   80    82  3      
HELIX   89    91  3      
TURN   93    98  6      
HELIX   102   115  14      
TURN   117   119  3      
HELIX   122   135  14      
TURN   136   138  3      
HELIX   156   159  4      
HELIX   169   177  9      
TURN   178   180  3      
HELIX   183   190  8      
HELIX   191   194  4      
STRAND   195   199  5      
HELIX   200   202  3      
HELIX   204   206  3      
STRAND   210   214  5      
HELIX   222   231  10      
STRAND   241   247  7      
STRAND   249   251  3      
HELIX   255   261  7      
HELIX   268   275  8      
TURN   277   283  7      
HELIX   284   292  9      
HELIX   294   308  15      
Sequence information
Length: 328 AA [This is the length of the unprocessed precursor] Molecular weight: 35023 Da [This is the MW of the unprocessed precursor] CRC64: DABD3854FB2D3B12 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKTQTKVMGG HVLLTVFTLC MLCSGVRAQL SPDIYAKSCP NLVQIVRKQV AIALKAEIRM 

        70         80         90        100        110        120 
AASLIRLHFH DCFVNGCDAS LLLDGADSEK LAIPNINSAR GFEVIDTIKA AVENACPGVV 

       130        140        150        160        170        180 
SCADILTLAA RDSVVLSGGP GWRVALGRKD GLVANQNSAN NLPSPFEPLD AIIAKFVAVN 

       190        200        210        220        230        240 
LNITDVVALS GAHTFGQAKC AVFSNRLFNF TGLGNPDATL ETSLLSNLQT VCPLGGNSNI 

       250        260        270        280        290        300 
TAPLDRSTTD TFDNNYFKNL LEGKGLLSSD QILFSSDLAV NTTKKLVEAY SRSQSLFFRD 

       310        320 
FTCAMIRMGN ISNGASGEVR TNCRVINN 

Q39034 in FASTA format

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