ID A0A0C9M2B8_9FUNG Unreviewed; 733 AA.
AC A0A0C9M2B8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN ORFNames=MAM1_0028d02268 {ECO:0000313|EMBL:GAN02821.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02821.1};
RN [1] {ECO:0000313|EMBL:GAN02821.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02821.1};
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: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927}.
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DR EMBL; DF836317; GAN02821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9M2B8; -.
DR STRING; 91626.A0A0C9M2B8; -.
DR OrthoDB; 3198922at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF3; CATALASE B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..733
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002214903"
FT DOMAIN 62..449
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 395
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:PIRSR038927-2"
SQ SEQUENCE 733 AA; 81693 MW; 8DBD18F362C8A252 CRC64;
MKASFITSFV SFFMAAQLVA AASNPSTDAT CALTGSTNDG SVNAKDEQLS QFTIVDNGGQ
ETSQFGVKIN NSDSLKAGLD GPGLMEDFQM REKIMHFDHE RIPERAVHAR AVGLHGYFES
YGDYSNITAA SFLREKGKKT PMFVRISTVL GSRGSPDTVR DVHGFALRFY TDEGLFDVVG
NNVPPFFVHD AIKFPDLIHA GKPQPDTETP QAGTAHETAY DFFAEFPETM HTVLWALSGR
GIPRSLRQIE GFGVHTFRLV NEQGASTYAK FVWKPKQGLS NLLWDEAQKI AGKDIDFHRN
DIYTAINKGD YPEWEWGVQL IPEEDFNKYD FSLLDPTKLV PESLVPFQPL GKMVLNRNPD
NYFAETEQVT FHPGHVVRGV GFTNDPLLQG RLFSYLDTQL NRMSGPNYMQ LPINRPLNVV
HNNQRDGFMQ MQIHKGKVAY FPNGLQGNTP SMVDSDKGGY IEYPEKINNV TKIRGRSSKF
FDFYSQPQLY YNSLTVAEKQ QLIDGLRFEI GKSASMDVRK RMINQLNHVD NDMARRIAYT
VGVDLPDKIV ENQNQTSVGL SIEEYPKAGN IKTRTVAILT APGSDNSDAQ AMYDFLEKKG
AYPAFVGIRQ GNQDGLNITE SYLTTSSVLW DAVYVPGGNK SLQVMTSRSS LFPYDEPKMF
VLDAFRHGKP IAASAEGSKL LEYAGVDMPA TGNSTAEMDG VIVADSEANT EKAFEDALIQ
QRYWSRLPLD PAI
//