ID CATA_SCHPO Reviewed; 512 AA.
AC P55306;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=cta1; ORFNames=SPCC757.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8537298; DOI=10.1093/oxfordjournals.jbchem.a124864;
RA Nakagawa C.W., Mutoh N., Hayashi Y.;
RT "Transcriptional regulation of catalase gene in the fission yeast
RT Schizosaccharomyces pombe: molecular cloning of the catalase gene and
RT northern blot analyses of the transcript.";
RL J. Biochem. 118:109-116(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13788.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D55675; BAA09526.1; -; Genomic_DNA.
DR EMBL; D89126; BAA13788.1; ALT_INIT; mRNA.
DR EMBL; CU329672; CAA21232.1; -; Genomic_DNA.
DR PIR; JC4164; JC4164.
DR PIR; T42369; T42369.
DR RefSeq; NP_587682.1; NM_001022677.2.
DR AlphaFoldDB; P55306; -.
DR SMR; P55306; -.
DR BioGRID; 275983; 14.
DR STRING; 284812.P55306; -.
DR PeroxiBase; 5261; SpomKat01.
DR iPTMnet; P55306; -.
DR MaxQB; P55306; -.
DR PaxDb; 4896-SPCC757-07c-1; -.
DR EnsemblFungi; SPCC757.07c.1; SPCC757.07c.1:pep; SPCC757.07c.
DR GeneID; 2539418; -.
DR KEGG; spo:SPCC757.07c; -.
DR PomBase; SPCC757.07c; -.
DR VEuPathDB; FungiDB:SPCC757.07c; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; P55306; -.
DR OMA; KFRWNVF; -.
DR PhylomeDB; P55306; -.
DR Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
DR PRO; PR:P55306; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:PomBase.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IMP:PomBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061692; P:cellular detoxification of hydrogen peroxide; IMP:PomBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:PomBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08157; catalase_fungal; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome.
FT CHAIN 1..512
FT /note="Catalase"
FT /id="PRO_0000084927"
FT REGION 488..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 344
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 512 AA; 58279 MW; 1F00ECE327C1AB08 CRC64;
MNSKDSNTVP VYTTNTGCPI FNPMAAARVG KGGPVLLQDS HLIDVFQHFD RERIPERVVH
AKGSGAFGEF ECTDDITKYT KHTMFSKVGK KTPMVARFST VGGERGTPDT ARDPRGFALK
FYTDEGIFDM VGNNTPVFFL RDPAKFPLFI HTQKRNPQND MKDATMFWDY LSQNAESIHQ
VMILFSDLGG TPYSYRFMDG FSSHTYKFVN DKGEFYYCKW HFITNQGTKG LTNEEAAALD
GSNPDHARQD LFEAIERGDY PSWTLYVQVM TPQEAEKYRY NIFDLTKVWP HKDVPMQRVG
RFTLNQNPTN FFADIEQAGF SPSHMVPGIE VSADPVLQVR TFSYPDTHRH RLGANFEQIP
VNSPKCPVFN YSRDGPMNVN GNQGNWPNYP SSIRPLAKVQ YEPDEGHEKW VGQVTYHMDE
ITDVDFEQPR AFWQNVLGKK PGQQDNFVKN VAGHLSGAIS PVRERQYGVF TRVDSELGRR
IREATEAEVK KMEEKAPKPI NKGEPHMFQG SS
//
