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Protein

Catalase isozyme 1

Gene

CAT1

Organism
Ricinus communis (Castor bean)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651PROSITE-ProRule annotation
Active sitei138 – 1381PROSITE-ProRule annotation
Metal bindingi348 – 3481Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. catalase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
  2. response to oxidative stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase isozyme 1 (EC:1.11.1.6)
Gene namesi
Name:CAT1
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Subcellular locationi

  1. Peroxisome Curated
  2. Glyoxysome Curated

GO - Cellular componenti

  1. glyoxysome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Glyoxysome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Catalase isozyme 1PRO_0000084956Add
BLAST

Proteomic databases

PRIDEiQ01297.

Expressioni

Tissue specificityi

Abundant in endosperms and cotyledons. Only in small amount in root.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliQ01297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

InParanoidiQ01297.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPYRNRPSS GFNTPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLIEK
60 70 80 90 100
LANFDRERIP ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI
110 120 130 140 150
VRFSTVIHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK
160 170 180 190 200
FPDVVHAFKP NPKSHLQENW RIFDFLSHVP ESLHMLTFLL DDLGIPQDYR
210 220 230 240 250
HMEGSGVNTY TLINKAGKVH YVKFHWKPTC GVKCLLENEA IKVGGSNHSH
260 270 280 290 300
ATQDLYDSIS AGNYPEWKLY IQIMDPAHED KFDFDPLDVT KTWPEDILPL
310 320 330 340 350
QPVGRLVLNK NIDNFFAENE QLAFCPGIVV PGVSYSEDKL LQTRIFSYSD
360 370 380 390 400
TQRHRLGPNY LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRCDPA
410 420 430 440 450
RNAESFPVPS AICSGKREKC VIEKENNFKQ PGERYRSWAP DRQERFLNRL
460 470 480 490
VGGLSDPRIT HELRTIWISY WIQCDKSLGQ KLATRLNVKP SI
Length:492
Mass (Da):56,464
Last modified:February 1, 1996 - v2
Checksum:iB5E28A425088BF63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391A → P in CAA42215 (PubMed:1712298).Curated
Sequence conflicti446 – 4461F → S in CAA42215 (PubMed:1712298).Curated
Sequence conflicti454 – 4541L → F (PubMed:1712298).Curated
Sequence conflicti456 – 4561D → E (PubMed:1712298).Curated
Sequence conflicti461 – 4611H → Q in CAA42215 (PubMed:1712298).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21161 Genomic DNA. Translation: BAA04697.1.
X59694 mRNA. Translation: CAA42215.1.
PIRiS46297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21161 Genomic DNA. Translation: BAA04697.1.
X59694 mRNA. Translation: CAA42215.1.
PIRiS46297.

3D structure databases

ProteinModelPortaliQ01297.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ01297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiQ01297.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCATA1_RICCO
AccessioniPrimary (citable) accession number: Q01297
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: March 4, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.