Reviewed, UniProtKB/Swiss-Prot Q96528 (CATA1_ARATH)

Names and origin

Protein names

Recommended name:
    Catalase-1
    EC=1.11.1.6

Gene names

Name:	CAT1
Ordered Locus Names:	At1g20630
ORF Names:	F2D10.11, F5M15.31

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	Cytoplasm Potential.
Sequence similarities	Belongs to the catalase family.
Sequence caution	The sequence AAF79625.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAF80611.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 response to abscisic acid stimulus Inferred from expression pattern. Source: TAIR response to cadmium ion Inferred from expression pattern. Source: TAIR response to light stimulus Inferred from expression pattern. Source: TAIR
Cellular component	cell wall Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR cytosolic ribosome Inferred from direct assay. Source: TAIR mitochondrion Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR
Molecular function	catalase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Catalase-1		PRO_0000084930
Sites
	Active site	65	1	By similarity
	Active site	138	1	By similarity
	Metal binding	348	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	103	1	F → L in AAB07026. Ref.1
	Sequence conflict	332	1	G → F in AAB07026. Ref.1
	Sequence conflict	339 – 340	2	KL → NV in AAB07026. Ref.1
	Sequence conflict	423	1	G → R Ref.1
	Sequence conflict	423	1	G → R Ref.2
	Sequence conflict	455	1	S → W in AAB07026. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96528-1 [UniParc]. Last modified July 11, 2002. Version 3. Checksum: 271E55FF7D6910EB	FASTA	492	56,762
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catalase is encoded by a multigene family in Arabidopsis thaliana (L.) Heynh." Frugoli J.A., Zhong H.H., Nuccio M.L., McCourt P., McPeek M.A., Thomas T.L., McClung C.R. Plant Physiol. 112:327-336(1996) [PubMed: 8819328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"Intron loss and gain during evolution of the catalase gene family in angiosperms." Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R. Genetics 149:355-365(1998) [PubMed: 9584109] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed: 11130712] [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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U43340 mRNA. Translation: AAB07026.1. AF021937 Genomic DNA. Translation: AAC17731.1. AC069251 Genomic DNA. Translation: AAF80611.1. Sequence problems. AC027665 Genomic DNA. Translation: AAF79625.1. Sequence problems. AY136424 mRNA. Translation: AAM97090.1. BT010373 mRNA. Translation: AAQ56816.1.
IPI	IPI00520908.
RefSeq	NP_564121.1.
UniGene	At.26213
3D structure databases
HSSP	HSSP built from PDB template 1M7S based on UniProtKB P46206.
ModBase	Search...
Protein family/group databases
PeroxiBase	5142. AtKat01.
Proteomic databases
PRIDE	Q96528.
ProMEX	Q96528.
Genome annotation databases
GeneID	838652.
GenomeReviews	Gene locus AT1G20630 in contig CT485782_GR.
KEGG	ath:AT1G20630.
NMPDR	fig|3702.1.peg.2412.
Organism-specific databases
TAIR	At1g20630.
Phylogenomic databases
OMA	Q96528. EPRVTHE.
Enzyme and pathway databases
BRENDA	1.11.1.6. 302.
Gene expression databases
ArrayExpress	Q96528.
GermOnline	AT1G20630. Arabidopsis thaliana.
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

CATA1_ARATH

Accession

Primary (citable) accession number: Q96528
Secondary accession number(s): O22529, Q9LDS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2002
Last modified:	June 16, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)