ID CATE_BACSU Reviewed; 686 AA.
AC P42234; P42309;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Catalase-2;
DE EC=1.11.1.6;
GN Name=katE; Synonyms=katB; OrderedLocusNames=BSU39050; ORFNames=N15D;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 524.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-536.
RX PubMed=7559348; DOI=10.1128/jb.177.19.5598-5605.1995;
RA Engelmann S., Lindner C., Hecker M.;
RT "Cloning, nucleotide sequence, and regulation of katE encoding a sigma B-
RT dependent catalase in Bacillus subtilis.";
RL J. Bacteriol. 177:5598-5605(1995).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide. Involved in
CC sporulation.
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 -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA59465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D83026; BAA11699.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15931.2; -; Genomic_DNA.
DR EMBL; X85182; CAA59465.1; ALT_FRAME; Genomic_DNA.
DR PIR; D69647; D69647.
DR RefSeq; NP_391784.2; NC_000964.3.
DR RefSeq; WP_003243331.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42234; -.
DR SMR; P42234; -.
DR STRING; 224308.BSU39050; -.
DR PeroxiBase; 4059; BsKat02_168.
DR PaxDb; 224308-BSU39050; -.
DR EnsemblBacteria; CAB15931; CAB15931; BSU_39050.
DR GeneID; 937481; -.
DR KEGG; bsu:BSU39050; -.
DR PATRIC; fig|224308.179.peg.4228; -.
DR eggNOG; COG0693; Bacteria.
DR eggNOG; COG0753; Bacteria.
DR InParanoid; P42234; -.
DR OrthoDB; 9760293at2; -.
DR PhylomeDB; P42234; -.
DR BioCyc; BSUB:BSU39050-MONOMER; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd08155; catalase_clade_2; 1.
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; 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; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Sporulation.
FT CHAIN 1..686
FT /note="Catalase-2"
FT /id="PRO_0000084970"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 365
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"
FT CONFLICT 524
FT /note="I -> N (in Ref. 1; BAA11699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 77480 MW; 1C74405B4310E091 CRC64;
MSDDQNKRVN EHSKDEQLEQ YRTDNSGKKM TTNQGLRVSE DEHSLKAGVR GPTLMEDFHF
REKMTHFDHE RIPERVVHAR GFGVHGFFQV YEPMTEYTRA KFLQDPSVKT PVFVRFSTVA
GSKGSADTVR DARGFATKFY TEEGNYDLVG NNIPVFFIQD AIKFPDLVHA FKPEPHNEMP
QAATAHDTFW DFVANNPESA HMVMWTMSDR GIPRSYRMME GFGVHTFRFV NEQGKARFVK
FHWKPVLGVH SLVWDEAQKI AGKDPDFHRR DLWETIENGG KVEYELGVQM IDEEDEFKFD
FDILDPTKLW PEELVPVKII GKMTLNRNQD NVFAETEQVA FHPGNVVPGI DFTNDPLLQG
RLFSYTDTQL IRLGGPNFHE IPINRPVCPF HNNQYDGYHR MTINKGPVAY HKNSLQNNDP
SPATAEEGGY VHYQEKVEGK KIRQRSDSFN DYYSQAKLFW NSMSPVEKQH IISAFCFEVG
KVKSKDVQRQ VVDVFSNVDA DLAEEIAKGV GVAAPAKRKA SKEILTSPAL SQARTVKTAS
TRKVAVLAGN GFHEKELQTV LEALKQEGIT VDIISQNLGY MTSGSGQQLE ASGTFLTVDS
VLYDAVYAAG GLELKDNKQA MAFIREAYNH YKAIGAANEG IDLLQSSVGT TEGLGIVTAK
DEPDYTAFSK AFIDAVAAHR HWDRRI
//
