KATG_SHEWM
ID KATG_SHEWM Reviewed; 736 AA.
AC B1KFI8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Swoo_3905;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-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; CP000961; ACA88163.1; -; Genomic_DNA.
DR RefSeq; WP_012326493.1; NC_010506.1.
DR AlphaFoldDB; B1KFI8; -.
DR SMR; B1KFI8; -.
DR STRING; 392500.Swoo_3905; -.
DR EnsemblBacteria; ACA88163; ACA88163; Swoo_3905.
DR KEGG; swd:Swoo_3905; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000002168; 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 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; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 22..736
FT /note="Catalase-peroxidase"
FT /id="PRO_5000316507"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 265
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 99
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 102..224
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 250)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 224..250
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 102)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 736 AA; 81474 MW; 1E411341E32F9B0A CRC64;
MFKKTILSFV ISAVMVTAAS AVENEQPKSN QFWWPNQLDL TPLRNHSDES NPQNSNFDYA
EAFEKLDLEA VKKDIDKVLT NSQDWWPADY GHYGPFFIRM AWHAAGTYRT HDGRGGAGGG
QQRFDPLNSW PDNVNLDKAR RLLWPIKQKY GQSISWADLI ALTGNVALES MGFKTYGYAG
GREDDWEPDL VYWGPESKFL TDERRDKKGK LKGPLAAVEM GLIYVNPVGP HGNPDPLLAA
NDIRMSFGRM AMNDEEIVAL IAGGHTFGKA HGAKKPTECV GPEPAAAAVE EQGFGWKNRC
GTGSGADTTS SGLEGAWTIT PTQWTTNYLD NLFTFNWVKT KSPAGAIQWI PDTDTAANLV
PDAHDPTKRH APIMFTTDIA IKEDPKFRAI AESFRKSPDK YELAFAKAWF KLNHRDLGPR
SRYLGNEVPK EVLVWQDPIP ELNHPVVNDA DIAKLKSEIL KSGLSVQDLV LTAWASASSY
RGTDMRGGAN GARINLSPQN EWQVNNPKQL AKVLNKLEKI KDKFNKKSKK AKISLADLIV
LGGAAAIEKS VKEAGFNNKV PFTPGRMDAS QAMTDVASFG VLESTADGFR NYYSDESNLS
PAQMLIDKAD LLTLTVPEMT ALVGGMRALS ANADGSNHGV FTDQPGVLSN DFFVNLLDMS
VKWSKKPKSE ALYEGYDRKT GKLKWTATPV DLVFGSNTEL RAISEFYASK NAEEQFITDF
IAAWHKVMVN DRFDIK
