ID A0A0C9LPX5_9FUNG Unreviewed; 725 AA.
AC A0A0C9LPX5;
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_0004c00526 {ECO:0000313|EMBL:GAN01095.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN01095.1};
RN [1] {ECO:0000313|EMBL:GAN01095.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN01095.1};
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; DF836293; GAN01095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LPX5; -.
DR STRING; 91626.A0A0C9LPX5; -.
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..725
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002199236"
FT DOMAIN 37..424
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 370
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 725 AA; 81324 MW; 1B3347AB1F72DA93 CRC64;
MKLVTLIIPL TVVAQCCLAQ KDPVGDAYVV DAGTTETTNF GAKINNTDSL TVGKRGPTLL
EDFQLREKIM HFDHERIPER VVHARGVGAH GYFQPYQDWS NITAAKFLQD PDVKTPTFVR
FSTVLGSRGS PDTVRDVRGF ATRFYTGEGN FDLVGNVIAP FFIQDAIKFP DLIHAGKPEP
DKEVPQAGTA HCTSYDFFAE HTESIHTVLW ALSGRGLVKS FRQVEGFGVH TFRLINEEGK
TVFVKFHWKP LQGLSNLVWD EAQKIAGKDI DYHRNDLYTA IEKGDYPEYE LGVQIVKPED
EDSFDFDLLD STKIIPESIV PVTKLGKMTL NRNVENYFSE TEQVTFHLGH IVRGITFTDD
PLLQGRLFSY LDTQINRMNS ANFLQLPINK PLVPVHNNQR DGYMQRNVYK GKVAYFPNKL
QDNTPAMANN KTDGYLEYPE HLNANKQRGK GGKYSDHYSQ AQLFWNSLTT PEQQQLVDAA
RFELGKCADN DVHKRMVQVF NHVDNNLAVR VAYALGVPEP KPVSKNEKKT SKGLSIENYP
KPNHIRTKKV AIFTAPGIDV SEAKTMFDFL DKEGAYPEYV GFKLGEQDGI VTNHTFLTTS
SVLYDAVYVP SGEKSAFQLL TDSVSAFPYN EPAVFLLDAY RHGKPIAASG RATTLLKAAQ
LPSEALNIST PKQKEIGVFV SSDAGSDLQN LFKEGIIQQR YWNRLPTDSN AEKSPTSTKK
MILQE
//
