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UniProtKB/Swiss-Prot entry Q96528


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

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Entry information
Entry name CATA1_ARATH
Primary accession number Q96528
Secondary accession numbers O22529 Q9LDS9
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 11, 2002 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Catalase-1
Synonym EC 1.11.1.6
Gene name
Name: CAT1
OrderedLocusNames: At1g20630
ORFNames: F2D10.11, F5M15.31
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. Landsberg erecta;
DOI=10.1104/pp.112.1.327; PubMed=8819328 [NCBI, ExPASy, EBI, Israel, Japan]
Frugoli J.A., Zhong H.H., Nuccio M.L., McCourt P., McPeek M.A., Thomas T.L., McClung C.R.;
"Catalase is encoded by a multigene family in Arabidopsis thaliana (L.) Heynh.";
Plant Physiol. 112:327-336(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9584109 [NCBI, ExPASy, EBI, Israel, Japan]
Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R.;
"Intron loss and gain during evolution of the catalase gene family in angiosperms.";
Genetics 149:355-365(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[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
U43340; AAB07026.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF021937; AAC17731.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC069251; AAF80611.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC027665; AAF79625.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136424; AAM97090.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT010373; AAQ56816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_564121.1; -.
UniGene At.26213
3D structure databases
HSSP P46206; 1M7S. [HSSP ENTRY / PDB]
ModBase Q96528.
Protein family/group databases
PeroxiBase 5142; AtKat01.
Organism-specific databases
TAIR At1g20630; -.
Gene expression databases
ArrayExpress Q96528; -.
GermOnline AT1G20630; Arabidopsis thaliana.
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.
BLOCKS Q96528.
Proteomic databases
ProMEX Q96528; -.
Genome annotation databases
GeneID 838652; -.
GenomeReviews CT485782_GR; AT1G20630.
KEGG ath:AT1G20630; -.
NMPDR fig|3702.1.peg.2412; -.
Other
ProtoNet Q96528.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   492  492     Catalase-1. PRO_0000084930
ACT_SITE   65    65        By similarity. 
ACT_SITE   138   138        By similarity. 
METAL   348   348        Iron (heme axial ligand) (By similarity). 
CONFLICT   103   103        F -> L (in Ref. 1; AAB07026). 
CONFLICT   332   332        G -> F (in Ref. 1; AAB07026). 
CONFLICT   339   340        KL -> NV (in Ref. 1; AAB07026). 
CONFLICT   423   423        G -> R (in Ref. 1 and 2). 
CONFLICT   455   455        S -> W (in Ref. 1; AAB07026). 
Sequence information
Length: 492 AA [This is the length of the unprocessed precursor] Molecular weight: 56762 Da [This is the MW of the unprocessed precursor] CRC64: 271E55FF7D6910EB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPYRVRPSS AHDSPFFTTN SGAPVWNNNS SLTVGTRGPI LLEDYHLLEK LANFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD ITQLTSADFL RGPGVQTPVI VRFSTVIHER GSPETLRDPR 

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

       190        200        210        220        230        240 
ESLHMFSFLF DDLGIPQDYR HMEGAGVNTY MLINKAGKAH YVKFHWKPTC GIKCLSDEEA 

       250        260        270        280        290        300 
IRVGGANHSH ATKDLYDSIA AGNYPQWNLF VQVMDPAHED KFDFDPLDVT KIWPEDILPL 

       310        320        330        340        350        360 
QPVGRLVLNK NIDNFFNENE QIAFCPALVV PGIHYSDDKL LQTRIFSYAD SQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRLDPV RHAEKYPTTP IVCSGNREKC 

       430        440        450        460        470        480 
FIGKENNFKQ PGERYRSWDS DRQERFVKRF VEALSEPRVT HEIRSIWISY WSQADKSLGQ 

       490 
KLATRLNVRP NF 

Q96528 in FASTA format

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