ID E1WX70_HALMS Unreviewed; 520 AA.
AC E1WX70;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=katB {ECO:0000313|EMBL:CBW25771.1};
GN OrderedLocusNames=BMS_0880 {ECO:0000313|EMBL:CBW25771.1};
OS Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS (Bacteriovorax marinus).
OC Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC Halobacteriovoraceae; Halobacteriovorax.
OX NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW25771.1, ECO:0000313|Proteomes:UP000008963};
RN [1] {ECO:0000313|Proteomes:UP000008963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC {ECO:0000313|Proteomes:UP000008963};
RX PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA Williams H.N., Stine O.C.;
RT "A small predatory core genome in the divergent marine Bacteriovorax
RT marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL ISME J. 7:148-160(2013).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC 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; FQ312005; CBW25771.1; -; Genomic_DNA.
DR RefSeq; WP_014243556.1; NC_016620.1.
DR AlphaFoldDB; E1WX70; -.
DR STRING; 862908.BMS_0880; -.
DR KEGG; bmx:BMS_0880; -.
DR PATRIC; fig|862908.3.peg.838; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_7; -.
DR Proteomes; UP000008963; Chromosome.
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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 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:UP000008963};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..520
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003154115"
FT DOMAIN 26..412
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 358
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 520 AA; 59254 MW; F39CD14CB4D451E3 CRC64;
MNIKKLSTTL VVLSTLSLPA HATTLTRETG APVGDNQNSK TAGPNGGVLL EDAHLIEKLA
RFDRMRIPER VVHARGTGAH GVFKSYGDFS KLTRASLFNR KNKKTPVFVR FSSVIHSKGS
PESLRDPRGF ATKFYTDQGN WDLVGNNLPV FFIRDAIKFP DMVNSLKPDP KTNKQDPNRI
FDFMAHHPES IHMWTHLMSN KGTPASLRTM DGNGVHAYKF VNKDNKVRYV KFRWVSKQGV
KNLTAKEAQK VQGEDFSYLT TDLYDNIKKG NYPSWELVAL VMELDQLDKH DFNPLDVTKD
WKCEMSSIEC TKLGLMTLNK VPTNFFQFTE QSAFSPAVFV PGIEPSEDRL LQGRLFAYSD
TQRYRLGVNY QYLPVNKAKV EINTYAQDGS LSTRVANEEH INYQPNHFDG SLNRDRGTLH
EDQQYKYSQH KLSGSTQQKM IAKTQNFKQA GETYRSYSDF DKEHLIKNFG GTLNQIKNKL
IVTQMIAYAY KADKEYGEKL AKFTNTDLNK VKSVVVKLRD
//
