ID A0A291GXU4_9MICO Unreviewed; 745 AA.
AC A0A291GXU4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CFK41_09405 {ECO:0000313|EMBL:ATG54956.1};
OS Brachybacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1331682 {ECO:0000313|EMBL:ATG54956.1, ECO:0000313|Proteomes:UP000217889};
RN [1] {ECO:0000313|EMBL:ATG54956.1, ECO:0000313|Proteomes:UP000217889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY80 {ECO:0000313|EMBL:ATG54956.1,
RC ECO:0000313|Proteomes:UP000217889};
RX PubMed=24944333; DOI=10.1099/ijs.0.058388-0;
RA Hoang V.A., Kim Y.J., Nguyen N.L., Yang D.C.;
RT "Brachybacterium ginsengisoli sp. nov., isolated from soil of a ginseng
RT field.";
RL Int. J. Syst. Evol. Microbiol. 64:3063-3068(2014).
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 ECO:0000256|RuleBase:RU000498};
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. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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DR EMBL; CP023564; ATG54956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GXU4; -.
DR KEGG; bgg:CFK41_09405; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000217889; Chromosome.
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 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; IPR024708; Catalase_AS.
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:SF1; 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; PS00438; CATALASE_2; 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}.
FT DOMAIN 72..460
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 116
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 204
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 402
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 406
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"
FT BINDING 413
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 745 AA; 80514 MW; AFFCD1C6D4E1D961 CRC64;
MRRTRTVAST ENASDPAPGR PSSRPPSLQE PTEPTGPLPP KSDQQGAQPR TPTGAEPGRE
PSTTAQQGEF LTTSQGARLR DTDHSLKAGR RGPVLLQDHH LREKITHFDH ERIPERVVHA
RGAAAHGVFE GYGTAEPVCR AGFLAKGVRT EVFTRFSTVV GSRGSMDTAR DTRGFATKFY
TEEGTFDLVG NNIPVFFIQD GMKFPDVVHA AKPHPDREIP QAQSAHDTFW DFVSLHTEAQ
HHTLWFMGDR GIPRSFRMME GFGVHTFRLS NSDGETSLAK LHWKPALGVH SLTWEEAQLL
GGADPDFHRR DLADAIESGA YPSWELGIQV FPDNAEQSFE GIDLLDPTKF VPEELAPVQP
VGRLTLDRNP RNYFAETEQV AFNPGHLVPG IDVTDDPLLQ VRLFSYVDTQ LTRLGGPNFA
QLPINRAHAP INDMLRDGYG QQGDHSGVAP YQPNSLDGGC PFLAGEMDGA LEDLPVVVPE
SVKERALSAT FEDHFSQARL FWRSMTPVER DHIVDAYSFE LAKCYEATIR ERQLQSLANI
DGELCARVAA ALGMTAPERT IPAEDGTDGA PVTSAPLSQL GARWPTDGRT IGIVVDPDGD
NSALLALHDA VVAASMTPIV IAPRGGEVAG VPVGRTFGTA ASAELDALLL AGNPLTAPDA
RPSVDPTAGA PSSGEVEPRV GTLIDDCWRH AKAMGAWGEG RTALAARTAP GGAGLVAGED
GRAVLSEIRT LLESHRVWER FPADA
//
