Q01297 (CATA1_RICCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase isozyme 1
EC=1.11.1.6

Gene names

Name:

CAT1

Organism

Ricinus communis (Castor bean) [Complete proteome]

Taxonomic identifier

3988 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Subcellular location	Peroxisome Potential. Glyoxysome Potential.
Tissue specificity	Abundant in endosperms and cotyledons. Only in small amount in root.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Glyoxysome Peroxisome
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
Cellular_component	glyoxysome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	catalase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Catalase isozyme 1		PRO_0000084956
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	439	1	A → P in CAA42215. Ref.2
	Sequence conflict	446	1	F → S in CAA42215. Ref.2
	Sequence conflict	454	1	L → F Ref.2
	Sequence conflict	456	1	D → E Ref.2
	Sequence conflict	461	1	H → Q in CAA42215. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q01297 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: B5E28A425088BF63	FASTA	492	56,464
	10 20 30 40 50 60 MDPYRNRPSS GFNTPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLIEK LANFDRERIP 70 80 90 100 110 120 ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR 130 140 150 160 170 180 GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDVVHAFKP NPKSHLQENW RIFDFLSHVP 190 200 210 220 230 240 ESLHMLTFLL DDLGIPQDYR HMEGSGVNTY TLINKAGKVH YVKFHWKPTC GVKCLLENEA 250 260 270 280 290 300 IKVGGSNHSH ATQDLYDSIS AGNYPEWKLY IQIMDPAHED KFDFDPLDVT KTWPEDILPL 310 320 330 340 350 360 QPVGRLVLNK NIDNFFAENE QLAFCPGIVV PGVSYSEDKL LQTRIFSYSD TQRHRLGPNY 370 380 390 400 410 420 LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRCDPA RNAESFPVPS AICSGKREKC 430 440 450 460 470 480 VIEKENNFKQ PGERYRSWAP DRQERFLNRL VGGLSDPRIT HELRTIWISY WIQCDKSLGQ 490 KLATRLNVKP SI

References

[1]	"Isolation and characterization of two tightly linked catalase genes from castor bean that are differentially regulated." Suzuki M., Ario T., Hattori T., Nakamura K., Asahi T. Plant Mol. Biol. 25:507-516(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Hypocotyl.
[2]	"The C-terminal domain of plant catalases. Implications for a glyoxysomal targeting sequence." Gonzalez E. Eur. J. Biochem. 199:211-215(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-492. Strain: cv. Hale.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21161 Genomic DNA. Translation: BAA04697.1. X59694 mRNA. Translation: CAA42215.1.
PIR	S46297.
3D structure databases
ProteinModelPortal	Q01297.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.40.180.10. 1 hit.
InterPro	IPR018028. Catalase. IPR020835. Catalase-like_dom. IPR024708. Catalase_AS. IPR024711. Catalase_clade1/3. IPR011614. Catalase_core. IPR002226. Catalase_haem_BS. IPR010582. Catalase_immune_responsive. [Graphical view]
PANTHER	PTHR11465. PTHR11465. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
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_RICCO

Accession

Primary (citable) accession number: Q01297

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program