UniProt: A0A0C9MHK0

Database: UniProt
Entry: A0A0C9MHK0_9FUNG

LinkDB:  A0A0C9MHK0_9FUNG 
Original site:  A0A0C9MHK0_9FUNG

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (21)   

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ID   A0A0C9MHK0_9FUNG        Unreviewed;       478 AA.
AC   A0A0C9MHK0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=MAM1_0135d06249 {ECO:0000313|EMBL:GAN06759.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06759.1};
RN   [1] {ECO:0000313|EMBL:GAN06759.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN06759.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; DF836424; GAN06759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9MHK0; -.
DR   STRING; 91626.A0A0C9MHK0; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT   DOMAIN          5..389
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         335
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:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   478 AA;  54160 MW;  14518CB96803615C CRC64;
     MAILTTSNGN PVDNDQTSIT AGPWGPVLLQ DFHLIDKLAH FDRERIPERV VHAKGAGAHG
     EFEVTHDITH LTKAKFLSEV GKKTPMFARF STVGGEKGSP DTARDPRGFA LKFYTEEGNL
     DIVGNNTPVF FIRDPSKFPD FIHTQKRNPR TNLKDPNAAW DFFSLSPETI HQQTILYSNH
     GTPDGFRHMH GFGSHTFKLV DKEGKFKYIK WHFKTKQGVK NLKPDEAAKL EGTNPDYATQ
     DLFESIERGD FPAWDVFIQI MEPKDAKTYR WNPFDVTKVW PHKDYPLHPV GKFTLNKNPD
     NYFAEVEQAA FSPSHLVPGV DTSADRLLQG RLFSYPDTHR HRLGVNYKQI PINAPKCEVN
     TYQRDGAMVV NGNYGSAANY GPNSVGGPVQ NNIVGSTFAA EEIEGLIGRF SYDVTDDDFA
     QAGNLYRLMD EENKDDLCKN IAGDLVKVRK EIVERQLPHF ERADPDYRQR IEKFMKEA
//

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