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UniProtKB/Swiss-Prot entry P25819


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

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Entry information
Entry name CATA2_ARATH
Primary accession number P25819
Secondary accession number O49615
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on December 13, 2001 (Sequence version 3)
Annotations were last modified on    October 14, 2008 (Entry version 87)
Name and origin of the protein
Protein name Catalase-2
Synonym EC 1.11.1.6
Gene name
Name: CAT2
Synonyms: CAT
OrderedLocusNames: At4g35090
ORFNames: M4E13.140
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;
PubMed=16669103 [NCBI, ExPASy, EBI, Israel, Japan]
Chevalier C., Yamaguchi J., McCourt P.;
"Nucleotide sequence of a cDNA for catalase from Arabidopsis thaliana.";
Plant Physiol. 99:1726-1728(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Zentgraf U., Zinkernagel I.;
"A gene encoding a catalase isoform from Arabidopsis thaliana.";
(er) Plant Gene Register PGR96-005.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[4]
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).
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
X64271; CAA45564.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X94447; CAA64220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022023; CAA17773.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161586; CAB80226.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY074301; AAL66998.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY113854; AAM44902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05779; T05779.
RefSeq NP_195235.1; -.
UniGene At.24350
3D structure databases
HSSP P46206; 1M7S. [HSSP ENTRY / PDB]
ModBase P25819.
Protein-protein interaction databases
IntAct P25819; -.
Protein family/group databases
PeroxiBase 5141; AtKat02.
Enzyme and pathway databases
BioCyc MetaCyc:AT4G35090-MON; -.
Organism-specific databases
TAIR At4g35090; -.
Gene expression databases
ArrayExpress P25819; -.
Family and domain databases
InterPro IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
Pfam graphical view of domain structure.
PRINTS PR00067; CATALASE.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P25819.
Proteomic databases
ProMEX P25819; -.
Genome annotation databases
GeneID 829661; -.
GenomeReviews CT486007_GR; AT4G35090.
NMPDR fig|3702.1.peg.21584; -.
Other
ProtoNet P25819.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Glyoxysome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   492  492     Catalase-2. PRO_0000084931
ACT_SITE   65    65        By similarity. 
ACT_SITE   138   138        By similarity. 
METAL   348   348        Iron (heme axial ligand) (By similarity). 
VARIANT   421   421  1     I -> V (in strain: cv. Landsberg erecta). 
CONFLICT   39    39        P -> L (in Ref. 1; CAA45564). 
CONFLICT   109   109        E -> A (in Ref. 1; CAA45564). 
CONFLICT   154   154        M -> I (in Ref. 1; CAA45564). 
CONFLICT   243   243        V -> L (in Ref. 1; CAA45564). 
Sequence information
Length: 492 AA [This is the length of the unprocessed precursor] Molecular weight: 56931 Da [This is the MW of the unprocessed precursor] CRC64: AB622230561FD79B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPYKYRPAS SYNSPFFTTN SGAPVWNNNS SMTVGPRGPI LLEDYHLVEK LANFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP 

       190        200        210        220        230        240 
ESLNMFTFLF DDIGIPQDYR HMDGSGVNTY MLINKAGKAH YVKFHWKPTC GVKSLLEEDA 

       250        260        270        280        290        300 
IRVGGTNHSH ATQDLYDSIA AGNYPEWKLF IQIIDPADED KFDFDPLDVT KTWPEDILPL 

       310        320        330        340        350        360 
QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGIHYSDDKL LQTRVFSYAD TQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRYDQV RHAEKYPTPP AVCSGKRERC 

       430        440        450        460        470        480 
IIEKENNFKE PGERYRTFTP ERQERFIQRW IDALSDPRIT HEIRSIWISY WSQADKSLGQ 

       490 
KLASRLNVRP SI 

P25819 in FASTA format

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