ID A0A0H3DS42_EDWTF Unreviewed; 515 AA.
AC A0A0H3DS42;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN OrderedLocusNames=ETAF_1272 {ECO:0000313|EMBL:ADM41386.1};
OS Edwardsiella tarda (strain FL6-60).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=718251 {ECO:0000313|EMBL:ADM41386.1, ECO:0000313|Proteomes:UP000002230};
RN [1] {ECO:0000313|Proteomes:UP000002230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL6-60 {ECO:0000313|Proteomes:UP000002230};
RA van Soest J.J., Henkel C.V., Jansen H.J., van den Hondel C.A.M.J.J.,
RA Bloemberg G.V., Meijer A.H., Spaink H.P.;
RT "Genome comparisons of Edwardsiella bacteria analysed using deep sequencing
RT technology.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM41386.1, ECO:0000313|Proteomes:UP000002230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL6-60 {ECO:0000313|EMBL:ADM41386.1,
RC ECO:0000313|Proteomes:UP000002230};
RX PubMed=22003892; DOI=10.1186/1471-2172-12-58;
RA van Soest J.J., Stockhammer O.W., Ordas A., Bloemberg G.V., Spaink H.P.,
RA Meijer A.H.;
RT "Comparison of static immersion and intravenous injection systems for
RT exposure of zebrafish embryos to the natural pathogen Edwardsiella tarda.";
RL BMC Immunol. 12:58-58(2011).
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; CP002154; ADM41386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H3DS42; -.
DR KEGG; etd:ETAF_1272; -.
DR PATRIC; fig|718251.5.peg.1313; -.
DR HOGENOM; CLU_010645_4_0_6; -.
DR Proteomes; UP000002230; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..515
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002607754"
FT DOMAIN 35..416
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:0000256|PIRSR:PIRSR038928-2"
SQ SEQUENCE 515 AA; 57757 MW; BB68363FEB563CAF CRC64;
MHIVNGINGL IAKKNVLFFL TSLAISPSVL ADTLTRDNGA PVGDNQNSQT AGPNGPVLLQ
DVQLLQKLQR FDRERVPERV VHARGTGAHG VFMPTADISD LTVAKVFTPG STTPVFVRFS
SVVHGTHSPE TLRDPRGFAT KFYTAEGNWD LVGNNFPTFF IRDAIKFPDM VHAFKPDPRT
NLDNDARRFD FFSHLPESTR TLTLLYSNEG TPLSYRNMDG NSVHAYKLIN DKGEVHYVKF
HWKTRQGIKN LDPQQVEQIQ GKDYSHMTQD LVTAINRGDY PKWDLYIQVL KPADLKNFDF
DPLDATKVWP DVPERKIGEM VLNKNPDNVF QETEQVAMAP SNLIPGIEPS EDKLLQGRLF
AYADTQFYRI GANGLSLPIN KPHSAVNNGN QDGQLNSGHT LDKGVNYQPS RIYPREELVS
SRYSQTPLSG TTQQSKIQRE QNFKQAGELY RSYSKKEQND LINSLGTSLT SADTVSKNIM
LSYFYKADKD YGTRLTSVAN GDLPTVKNLA DKLQD
//
