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Database: UniProt
Entry: A0A3M8LDP3_9MICO
LinkDB: A0A3M8LDP3_9MICO
Original site: A0A3M8LDP3_9MICO 
ID   A0A3M8LDP3_9MICO        Unreviewed;       496 AA.
AC   A0A3M8LDP3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=EEJ31_06420 {ECO:0000313|EMBL:RNE63601.1};
OS   Cryobacterium tepidiphilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=2486026 {ECO:0000313|EMBL:RNE63601.1, ECO:0000313|Proteomes:UP000279859};
RN   [1] {ECO:0000313|EMBL:RNE63601.1, ECO:0000313|Proteomes:UP000279859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-85 {ECO:0000313|EMBL:RNE63601.1,
RC   ECO:0000313|Proteomes:UP000279859};
RA   Wang Y.;
RT   "Cryobacterium sp. nov., isolated from rhizosphere soil of lettuce.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RNE63601.1}.
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DR   EMBL; RDSR01000008; RNE63601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8LDP3; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000279859; 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:UP000279859}.
FT   DOMAIN          6..389
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        53
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   496 AA;  54906 MW;  5A46116BA8DACFCC CRC64;
     MTERTTTQTG TPVASDAHSL TAGANGVTAL HDRYLVEKLA QFNRERIPER IVHAKGGGAF
     GEFVVTEDVS RFTKAAVFQP GATTETLQRF SSVAGEMGSP DTWRDVRGFS VKFYTTEGNY
     DIVGNNTPVF FIRDGIKFPD FIHSQKRLPG SGLRDADMQW DFWTLSPESA HQVTYVMGDR
     GLPRTWREMP GFGSHTYQWI NADGERFWVK YHFTSNQGNS EMEGSEAEFI AGADADYYRR
     DLYEAIERGD FPSWDVHVQV MPYDDAKSYR FNPFDLTKVW PHADYPLIKV GTHTLNRNPE
     NFFAQIEQAA FSPANTVPGI DISPDKMLMA RVFSYPDAQR YRVGANFNQL PVNAPKAPVH
     NYSQDGAARH GFNPASTPVY APNSFGGPTA DAAAAGEGSW ESDGDLVRSA ATLHSEDSDF
     GQAGTLYREV FDAAAKERFL ETITGGISGV TRPEIVERAI WYWTQVDAEL GAALRANLAS
     TSETANEAAE YVGVAE
//
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