(data stored in ACNUC7421 zone)

SWISSPROT: Q751G2_ASHGO

ID   Q751G2_ASHGO            Unreviewed;       507 AA.
AC   Q751G2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=AGOS_AGL256W {ECO:0000313|EMBL:AAS54235.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54235.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54235.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|RuleBase:RU004142}.
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: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; AE016820; AAS54235.1; -; Genomic_DNA.
DR   RefSeq; NP_986411.1; NM_211473.2.
DR   SMR; Q751G2; -.
DR   STRING; 33169.AAS54235; -.
DR   PeroxiBase; 5263; AgoKat01.
DR   EnsemblFungi; AAS54235; AAS54235; AGOS_AGL256W.
DR   GeneID; 4622704; -.
DR   KEGG; ago:AGOS_AGL256W; -.
DR   HOGENOM; HOG000087852; -.
DR   InParanoid; Q751G2; -.
DR   KO; K03781; -.
DR   OMA; HADFGRM; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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; Q751G2.
DR   SWISS-2DPAGE; Q751G2.
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:UP000000591}.
FT   DOMAIN          20..408
FT                   /note="Catalase"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   METAL           352
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   507 AA;  57292 MW;  77E6C90675683BE2 CRC64;
     MAGNNDKTNS AEVREDRVVT NSVGNPINEP FATQRVGQHG PLLLQDYNLL DLLAHFNRER
     VPERNPHAHG SGAFGYFEVT DDITDVCGSA MFGEVGKRTR ALVRFSTVGG EKGSADTVRD
     PRGFAVKFYT EEGNLDWVYN NTPVFFIRDP SKFPHFIHTQ KRNPRTNLKD ANMFWDFLTT
     PENQVAIHQV MILFSDRGIP ASYRHMNGYS GHTYKWSNKQ GDWRYVQVHI KTDQGIKNLT
     AEEGAKLAGE DPDFCQQDLV QALERGEYPS WTVYIQTMTE EQAQKLPFSV FDLTKVWPHK
     DFPLRRVGRL VLNEVPTNFF AQIEQAAFSP ATTVPYQEPS ADPVLQARLF SYADAHRYRI
     GPNYHQVPVN CPYASKFFNP AIRDGPMNVD GNLGSEPNYL ATNNNYRFLG ADRPIQQHQE
     TWQGPAQPVH WATTGDIDFA QATALYHVLG RTPGQQRNLA HNVAIHVASA DPPIQERVFQ
     MFSRVDKGLG EAIRSEATAL SQKKPKL
//

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