Reviewed, UniProtKB/Swiss-Prot P25819 (CATA2_ARATH)

Names and origin

Protein names

Recommended name:
    Catalase-2
    EC=1.11.1.6

Gene names

Name:	CAT2
Synonyms:	CAT
Ordered Locus Names:	At4g35090
ORF Names:	M4E13.140

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group.
Subunit structure	Homotetramer and heterotetramer. At least six or seven isozymes are produced from a mixture of 3 gene products.
Subcellular location	Peroxisome. Glyoxysome.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Glyoxysome Peroxisome
Coding sequence diversity	Alternative splicing
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell death Inferred from mutant phenotype. Source: TAIR cell redox homeostasis Inferred from mutant phenotype. Source: TAIR cellular response to nitrogen starvation Inferred from expression pattern. Source: TAIR cellular response to phosphate starvation Inferred from expression pattern. Source: TAIR cellular response to sulfate starvation Inferred from expression pattern. Source: TAIR hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW photoperiodism Inferred from mutant phenotype. Source: TAIR response to cold Inferred from expression pattern. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR cytosolic ribosome Inferred from direct assay. Source: TAIR glyoxysome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: TAIR stromule Inferred from direct assay. Source: TAIR
Molecular function	catalase activity Inferred from mutant phenotype. Source: TAIR heme binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRL1	Q9ZPS9	1	EBI-1537161,EBI-2292728

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P25819-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Catalase-2		PRO_0000084931
Sites
	Active site	65	1	By similarity
	Active site	138	1	By similarity
	Metal binding	348	1	Iron (heme axial ligand) By similarity
Natural variations
	Natural variant	421	1	I → V in strain: cv. Landsberg erecta.
Experimental info
	Sequence conflict	39	1	P → L in CAA45564. Ref.1
	Sequence conflict	109	1	E → A in CAA45564. Ref.1
	Sequence conflict	154	1	M → I in CAA45564. Ref.1
	Sequence conflict	243	1	V → L in CAA45564. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 13, 2001. Version 3. Checksum: AB622230561FD79B	FASTA	492	56,931
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA for catalase from Arabidopsis thaliana." Chevalier C., Yamaguchi J., McCourt P. Plant Physiol. 99:1726-1728(1992) [PubMed: 16669103] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"A gene encoding a catalase isoform from Arabidopsis thaliana." Zentgraf U., Zinkernagel I. Plant Gene Register PGR96-005 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." 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. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64271 mRNA. Translation: CAA45564.1. X94447 Genomic DNA. Translation: CAA64220.1. AL022023 Genomic DNA. Translation: CAA17773.1. AL161586 Genomic DNA. Translation: CAB80226.1. AY074301 mRNA. Translation: AAL66998.1. AY113854 mRNA. Translation: AAM44902.1.
IPI	IPI00520641.
PIR	T05779.
RefSeq	NP_195235.1.
UniGene	At.24350 At.64718
3D structure databases
HSSP	HSSP built from PDB template 1M7S based on UniProtKB P46206.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25819. 3 interactions.
STRING	P25819.
Protein family/group databases
PeroxiBase	5141. AtKat02.
Proteomic databases
PRIDE	P25819.
ProMEX	P25819.
Genome annotation databases
GeneID	829661.
GenomeReviews	Gene locus AT4G35090 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.21584.
Organism-specific databases
TAIR	At4g35090.
Phylogenomic databases
OMA	SSINYEP.
Enzyme and pathway databases
BioCyc	MetaCyc:AT4G35090-MON.
BRENDA	1.11.1.6. 302.
Gene expression databases
ArrayExpress	P25819.
Genevestigator	P25819.
Family and domain databases
InterPro	IPR002226. Catalase. IPR010582. Catalase-rel_immune_responsive. IPR011614. Catalase_N. IPR018028. Catalase_rel_subgroup. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PRINTS	PR00067. CATALASE.
ProDom	PD000510. Catalase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA2_ARATH

Accession

Primary (citable) accession number: P25819
Secondary accession number(s): O49615

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 13, 2001
Last modified:	November 3, 2009
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)