KATG_CLOBB
ID KATG_CLOBB Reviewed; 730 AA.
AC B2TJE9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=CLL_A1367;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
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=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; CP001056; ACD21810.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TJE9; -.
DR SMR; B2TJE9; -.
DR PeroxiBase; 6254; CboCP01.
DR EnsemblBacteria; ACD21810; ACD21810; CLL_A1367.
DR KEGG; cbk:CLL_A1367; -.
DR PATRIC; fig|935198.13.peg.1314; -.
DR HOGENOM; CLU_025424_2_0_9; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000001195; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..730
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354764"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 259
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT SITE 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 95..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 730 AA; 82089 MW; 0EBD9CB4530E3A38 CRC64;
MTENKCPVTG KMGKATAGSG TTNKDWWPNQ LNLNILHQNS QLSNPMSKDF NYAEEFKKLD
FQALKVDLYM LMTDSQIWWP ADYGNYGPLF IRMAWHSAGT YRVGDGRGGG SLGLQRFAPL
NSWPDNINLD KARRLLWPIK KKYGNKISWA DLLILTGNCA LESMGLKTLG FGGGRVDVWE
PQEDIYWGSE KEWLGDEREK GDKELENPLA AVQMGLIYVN PEGPNGNPDP LGSAHDVRET
FARMAMNDEE TVALIAGGHT FGKCHGAASP SYVGPAPEAA PIEEQGLGWK NTYGSGNGDD
TIGSGLEGAW KANPTKWTMG YLKTLFKYDW ELVKSPAGAY QWLAKNVDEE DMVIDAEDST
KKHRPMMTTA DLGLRYDPIY EPIARNYLKN PEKFAHDFAS AWFKLTHRDM GPISRYLGPE
VPKESFIWQD PIPLVKHKLI TKKDITHIKK KILDSGLSIS DLVATAWASA STFRGSDKRG
GANGGRIRLE PQKNWEVNEP KKLNNVLNTL KQIKENFNSS HSKDKKVSLA DIIILGGCVG
IEQAAKRAGY NINVPFIPGR TDAIQEQTDV KSFAVLEPKE DGFRNYLKTK YVVKPEDMLI
DRAQLLTLTA PEMTVLIGGM RVLNCNYNKS KDGVFTNRPE CLTNDFFVNL LDMNTVWKPK
SEDKDRFEGF DRETGELKWT ATRVDLIFGS NSQLRAIAEV YACDDNKEKF IQDFIFAWNK
IMNADRFEIK
