(data stored in ACNUC6288 zone)

SWISSPROT: Q6BLU7_DEBHA

ID   Q6BLU7_DEBHA            Unreviewed;       485 AA.
AC   Q6BLU7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   OrderedLocusNames=DEHA2F10582g {ECO:0000313|EMBL:CAG89167.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89167.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89167.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000256|RuleBase:RU004142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240;
CC         EC=1.11.1.6; Evidence={ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CR382138; CAG89167.1; -; Genomic_DNA.
DR   RefSeq; XP_460824.1; XM_460824.1.
DR   STRING; 4959.XP_460824.1; -.
DR   PeroxiBase; 5257; DhKat02.
DR   EnsemblFungi; CAG89167; CAG89167; DEHA2F10582g.
DR   GeneID; 2904338; -.
DR   KEGG; dha:DEHA2F10582g; -.
DR   HOGENOM; HOG000087852; -.
DR   InParanoid; Q6BLU7; -.
DR   KO; K03781; -.
DR   OMA; HADFGRM; -.
DR   OrthoDB; 507937at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001315; P:age-dependent response to reactive oxygen species; IEA:EnsemblFungi.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.180.10; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 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; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLU7.
DR   SWISS-2DPAGE; Q6BLU7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Heme {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN        6    392       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     53     53       {ECO:0000256|PIRSR:PIRSR038928-1}.
FT   ACT_SITE    126    126       {ECO:0000256|PIRSR:PIRSR038928-1}.
FT   METAL       336    336       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038928-2}.
SQ   SEQUENCE   485 AA;  54871 MW;  F2E6F9B514A63977 CRC64;
     MAPVYTNSNG CPIPEPFATQ RVGQHGPLLL QDFNLIDSLA HFDRERIPER VVHAKGSGAY
     GYFEVTDDIS DVCSAAFLDT IGKKTKVLTR FSTVGGESGS ADSARDPRGF STKLYTEEGN
     LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDPTMF WDYLTSNQES IHQVMTLFSD
     RGTPASYREM NGYSGHTYKW SNKKGEWYYV QVHFISDQGV KTLTNEEAGE LAGSNPDFAQ
     EDLFKEIAKG NAPSWTCYIQ TMTQEQAKKA PFSVFDLTKV WPHKDYPMRR FGKLVLNENP
     KNYFAEIEQA AFAPAHTVPY MEASADPVLQ SRLFSYADTH RHRLGTNYTQ IPVNCPITGR
     VFNPHMRDGG MNVNGNLGSH PNYLATSKPV EFKNFSIQEE QEVWEGAACP FHWKCTDKDY
     SQATALYNVL AKYPNQQKNL AHNVAVHVSG AETHIQDKVF DMFAKVHPEL SANIKKEALQ
     LSPRK
//

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