Reviewed, UniProtKB/Swiss-Prot Q42547 (CATA3_ARATH)

Names and origin

Protein names

Recommended name:
    Catalase-3
    EC=1.11.1.6

Gene names

Name:	CAT3
Ordered Locus Names:	At1g20620
ORF Names:	F2D10.40, F5M15.5

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 H(2)O(2) = O(2) + 2 H(2)O.
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	PeroxisomePotential.
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	Peroxisome
Coding sequence diversity	Alternative splicing
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

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

Isoform 1 (identifier: Q42547-1)

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-3		PRO_0000084932
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	109	1	E → G Ref.1 Ref.2 Ref.3
	Sequence conflict	162	1	P → R Ref.1 Ref.2 Ref.3
	Sequence conflict	260	1	A → V in AAM65021. Ref.6
	Sequence conflict	468	1	I → T Ref.1 Ref.2 Ref.3
	Sequence conflict	472 – 473	2	SQ → LK Ref.1 Ref.2 Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 11, 2002. Version 3. Checksum: 7322B111CFEBF37E	FASTA	492	56,695
	10 20 30 40 50 60 MDPYKYRPSS AYNAPFYTTN GGAPVSNNIS SLTIGERGPV LLEDYHLIEK VANFTRERIP 70 80 90 100 110 120 ERVVHARGIS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVVHER ASPETMRDIR 130 140 150 160 170 180 GFAVKFYTRE GNFDLVGNNT PVFFIRDGIQ FPDVVHALKP NPKTNIQEYW RILDYMSHLP 190 200 210 220 230 240 ESLLTWCWMF DDVGIPQDYR HMEGFGVHTY TLIAKSGKVL FVKFHWKPTC GIKNLTDEEA 250 260 270 280 290 300 KVVGGANHSH ATKDLHDAIA SGNYPEWKLF IQTMDPADED KFDFDPLDVT KIWPEDILPL 310 320 330 340 350 360 QPVGRLVLNR TIDNFFNETE QLAFNPGLVV PGIYYSDDKL LQCRIFAYGD TQRHRLGPNY 370 380 390 400 410 420 LQLPVNAPKC AHHNNHHEGF MNFMHRDEEI NYYPSKFDPV RCAEKVPTPT NSYTGIRTKC 430 440 450 460 470 480 VIKKENNFKQ AGDRYRSWAP DRQDRFVKRW VEILSEPRLT HEIRGIWISY WSQADRSLGQ 490 KLASRLNVRP SI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The circadian clock gates expression of two Arabidopsis catalase genes to distinct and opposite circadian phases." Zhong H.H., McClung C.R. Mol. Gen. Genet. 251:196-203(1996) [PubMed: 8668130] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	Zhong H.H., McClung C.R. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 457 AND 492.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U43147 Genomic DNA. Translation: AAC49807.1. AF021937 Genomic DNA. Translation: AAC17732.1. AC069251 Genomic DNA. Translation: AAF80611.1. Sequence problems. AC027665 Genomic DNA. Translation: AAF79625.1. Sequence problems. AY058104 mRNA. Translation: AAL24212.1. AY056447 mRNA. Translation: AAL08303.1. AY087477 mRNA. Translation: AAM65021.1.
PIR	S71112.
RefSeq	NP_564120.1.
UniGene	At.24821
3D structure databases
HSSP	HSSP built from PDB template 1M7S based on UniProtKB P46206.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q42547.
Protein family/group databases
PeroxiBase	5143. AtKat03.
Proteomic databases
ProMEX	Q42547.
Genome annotation databases
GeneID	838651.
GenomeReviews	Gene locus AT1G20620 in contig CT485782_GR.
NMPDR	fig|3702.1.peg.2410.
Organism-specific databases
TAIR	At1g20620.
Gene expression databases
ArrayExpress	Q42547.
Family and domain databases
InterPro	IPR002226. Catalase. IPR011614. Catalase_N. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 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. False negative. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA3_ARATH

Accession

Primary (citable) accession number: Q42547
Secondary accession number(s): Q93VY9, Q9LDS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2002
Last modified:	November 25, 2008
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)