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Protein

Catalase

Gene

cta1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 sitei60 – 601PROSITE-ProRule annotation
Active sitei133 – 1331PROSITE-ProRule annotation
Metal bindingi344 – 3441Iron (heme axial ligand)By similarity

GO - Molecular functioni

  • catalase activity Source: PomBase
  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • cellular response to oxidative stress Source: PomBase
  • hydrogen peroxide catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-3299685. Detoxification of Reactive Oxygen Species.
R-SPO-74259. Purine catabolism.

Protein family/group databases

PeroxiBasei5261. SpomKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:cta1
ORF Names:SPCC757.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC757.07c.
PomBaseiSPCC757.07c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512CatalasePRO_0000084927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei363 – 3631Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP55306.

PTM databases

iPTMnetiP55306.

Interactioni

Protein-protein interaction databases

BioGridi275983. 6 interactions.
MINTiMINT-4690996.

Structurei

3D structure databases

ProteinModelPortaliP55306.
SMRiP55306. Positions 6-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

HOGENOMiHOG000087852.
InParanoidiP55306.
KOiK03781.
OMAiQERCIAM.
OrthoDBiEOG7K9KBN.
PhylomeDBiP55306.

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.

P55306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSKDSNTVP VYTTNTGCPI FNPMAAARVG KGGPVLLQDS HLIDVFQHFD
60 70 80 90 100
RERIPERVVH AKGSGAFGEF ECTDDITKYT KHTMFSKVGK KTPMVARFST
110 120 130 140 150
VGGERGTPDT ARDPRGFALK FYTDEGIFDM VGNNTPVFFL RDPAKFPLFI
160 170 180 190 200
HTQKRNPQND MKDATMFWDY LSQNAESIHQ VMILFSDLGG TPYSYRFMDG
210 220 230 240 250
FSSHTYKFVN DKGEFYYCKW HFITNQGTKG LTNEEAAALD GSNPDHARQD
260 270 280 290 300
LFEAIERGDY PSWTLYVQVM TPQEAEKYRY NIFDLTKVWP HKDVPMQRVG
310 320 330 340 350
RFTLNQNPTN FFADIEQAGF SPSHMVPGIE VSADPVLQVR TFSYPDTHRH
360 370 380 390 400
RLGANFEQIP VNSPKCPVFN YSRDGPMNVN GNQGNWPNYP SSIRPLAKVQ
410 420 430 440 450
YEPDEGHEKW VGQVTYHMDE ITDVDFEQPR AFWQNVLGKK PGQQDNFVKN
460 470 480 490 500
VAGHLSGAIS PVRERQYGVF TRVDSELGRR IREATEAEVK KMEEKAPKPI
510
NKGEPHMFQG SS
Length:512
Mass (Da):58,279
Last modified:October 1, 1996 - v1
Checksum:i1F00ECE327C1AB08
GO

Sequence cautioni

The sequence BAA13788.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55675 Genomic DNA. Translation: BAA09526.1.
D89126 mRNA. Translation: BAA13788.1. Different initiation.
CU329672 Genomic DNA. Translation: CAA21232.1.
PIRiJC4164.
T42369.
RefSeqiNP_587682.1. NM_001022677.2.

Genome annotation databases

EnsemblFungiiSPCC757.07c.1; SPCC757.07c.1:pep; SPCC757.07c.
GeneIDi2539418.
KEGGispo:SPCC757.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55675 Genomic DNA. Translation: BAA09526.1.
D89126 mRNA. Translation: BAA13788.1. Different initiation.
CU329672 Genomic DNA. Translation: CAA21232.1.
PIRiJC4164.
T42369.
RefSeqiNP_587682.1. NM_001022677.2.

3D structure databases

ProteinModelPortaliP55306.
SMRiP55306. Positions 6-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275983. 6 interactions.
MINTiMINT-4690996.

Protein family/group databases

PeroxiBasei5261. SpomKat01.

PTM databases

iPTMnetiP55306.

Proteomic databases

MaxQBiP55306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC757.07c.1; SPCC757.07c.1:pep; SPCC757.07c.
GeneIDi2539418.
KEGGispo:SPCC757.07c.

Organism-specific databases

EuPathDBiFungiDB:SPCC757.07c.
PomBaseiSPCC757.07c.

Phylogenomic databases

HOGENOMiHOG000087852.
InParanoidiP55306.
KOiK03781.
OMAiQERCIAM.
OrthoDBiEOG7K9KBN.
PhylomeDBiP55306.

Enzyme and pathway databases

ReactomeiR-SPO-3299685. Detoxification of Reactive Oxygen Species.
R-SPO-74259. Purine catabolism.

Miscellaneous databases

PROiP55306.

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

« Hide 'large scale' publications
  1. "Transcriptional regulation of catalase gene in the fission yeast Schizosaccharomyces pombe: molecular cloning of the catalase gene and northern blot analyses of the transcript."
    Nakagawa C.W., Mutoh N., Hayashi Y.
    J. Biochem. 118:109-116(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: PR745.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCATA_SCHPO
AccessioniPrimary (citable) accession number: P55306
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.