ID A0A239E5J8_9MICO Unreviewed; 489 AA.
AC A0A239E5J8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=SAMN06309944_0088 {ECO:0000313|EMBL:SNS39729.1};
OS Micrococcales bacterium KH10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales.
OX NCBI_TaxID=1945885 {ECO:0000313|EMBL:SNS39729.1, ECO:0000313|Proteomes:UP000198369};
RN [1] {ECO:0000313|EMBL:SNS39729.1, ECO:0000313|Proteomes:UP000198369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH10 {ECO:0000313|EMBL:SNS39729.1,
RC ECO:0000313|Proteomes:UP000198369};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZPE01000001; SNS39729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239E5J8; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000198369; 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:UP000198369}.
FT DOMAIN 7..391
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 336
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 489 AA; 55019 MW; A6540D853FF0D748 CRC64;
MTSQPTTNDF GAPVGSDQHS LTVGPNGPVL LHDHYLVEKL AHFNRERVPE RVVHAKGAGA
FGTFKVTADV SKYTKAAVFQ PGAETETLLR FSTVAGEQGS PDTWRDPRGF ALKFYTTEGN
YDLVGNNTPV FFIRDAIQFP DFIHSQKRRS QSGLRDNNMQ WDFWTQVPAS AHQVTWLMGD
RGIPRTWRHM DGFGSHTYQW INAAGEKFWV KYHFKTQQGI EFFTQDEADH KAGTDPDYHR
ADLFNSIEAG DFPRWTLKVQ IMPYDEARTY RFNPFDLTKV WSQKDYPLIE VGVLELNRNP
QDFFSEIEQA AFSPSSLVPG IGLSPDKMLL GRVFAYPDTH RYRIGANYAK LPVNAPHATT
TSSYSRDGAM NPHNYPASQP EYAPNSFGGP HADVSLVTEA DAWTADTEFV RQAYTLRPDD
NDFIQAGTLV REVLDDAARD RLVSNISGHV VAVTDGAILE RVFQYWKNVD ADLGARVESV
VRAAKQAQN
//