ID   CATE_ALKPO              Reviewed;         678 AA.
AC   P30266; D3FQA8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katE; Synonyms=katA; OrderedLocusNames=BpOF4_07610;
OS   Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS   (Bacillus pseudofirmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX   NCBI_TaxID=398511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX   PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA   Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA   Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA   Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA   Hu F.Z., Krulwich T.A.;
RT   "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT   support the ability to grow in an external pH range from 7.5 to 11.4.";
RL   Environ. Microbiol. 13:3289-3309(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-448.
RA   Quirk P.G., Krulwich T.A.;
RL   Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP001878; ADC49580.1; -; Genomic_DNA.
DR   EMBL; L02551; AAA22558.1; -; Genomic_DNA.
DR   PIR; S27490; S27490.
DR   RefSeq; WP_012960851.1; NC_013791.2.
DR   AlphaFoldDB; P30266; -.
DR   SMR; P30266; -.
DR   STRING; 398511.BpOF4_07610; -.
DR   EnsemblBacteria; ADC49580; ADC49580; BpOF4_07610.
DR   KEGG; bpf:BpOF4_07610; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_3_0_9; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; 1584770at2; -.
DR   Proteomes; UP000001544; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 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; PTHR42821; 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; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 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   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase; Reference proteome.
FT   CHAIN           1..678
FT                   /note="Catalase"
FT                   /id="PRO_0000084969"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         362
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:0000250"
SQ   SEQUENCE   678 AA;  77067 MW;  9173B10EB69C521E CRC64;
     MSNEREMQNK KDQQLESFRV EDEGKKLTTN QGLKVSEDEF SLKAGERGPT LMEDFHFREK
     MTHFDHERIP ERIVHARGFA AHGEFQVYDS MKEFTKAKFL QDPSVKTPVF VRFSTVAGSK
     GSAETVRDAR GFATKFYTEE GNYDLVGNNI PVFFIQDAIK FPDLVHALKP EPHNEIPQAQ
     SAHDTFWDFI ANNQESAHMV MWAMSDRSIP RSFRMMEGFG VHTFRFVNEE GKAHFVKFHW
     KPVLGIHSLV WDEAQKIAGK DPDFHRRDLW ESIENGDYPE YELGVQLISE EDEFNFDFDV
     LDPTKIWPEE EVPVKIIGKM TLNRNVDNVF AETEQVAFHP GHVVPGIDFT NDPLLQGRLF
     SYTDTQLIRL GGPNFHELPI NRPVCPFHNN QRDGYGRQTI NKGQVSYHKN SLAANTPQPA
     SEEEGGYAHY QEKVEGRKVR KRSESFKDHF SQAKLFWNSM SEVEKNHIIE AFSFELGKVQ
     SKSVQQQVVE MFAHVTSDLA KPVAEAIGAN LPQSEGSSVT KSSLALSQEN TIKKPDTRKV
     GVIIDNGFNG DEVKQVLNEL QSKGIQAEFI SDKLGIKKCA GGSEIEIDHT FLTGESVLFD
     ALYVVGGKEV DPSFKDDAVY FIKEAYAHFK PIGATHVGIK WLEEQEIVEK EGVVTGTDMN
     IFSQNLTGAV MEHRHWNR