KATG_SHEDO
ID KATG_SHEDO Reviewed; 720 AA.
AC Q12PF6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Sden_1384;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-2006) 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; CP000302; ABE54670.1; -; Genomic_DNA.
DR RefSeq; WP_011495828.1; NC_007954.1.
DR AlphaFoldDB; Q12PF6; -.
DR SMR; Q12PF6; -.
DR STRING; 318161.Sden_1384; -.
DR PeroxiBase; 2713; SdeCP01.
DR PRIDE; Q12PF6; -.
DR EnsemblBacteria; ABE54670; ABE54670; Sden_1384.
DR KEGG; sdn:Sden_1384; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; KWTATRM; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001982; 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; 2.
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..720
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354917"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 263
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 91
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 94..222
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 248)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 222..248
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 94)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 720 AA; 80755 MW; 776975A1B1174F09 CRC64;
MSENKCPVMH GSATTTENSM ANMNWWPKSL SLDILHQHDH KTNPMAADFN YQDEVKKLDF
VALKNDLHAL MTDSQAWWPA DWGHYGGLMI RLTWHAAGTY RIADGRGGAG HGSQRFAPLN
SWPDNGNLDK ARRLLWPIKK KYGNKLSWAD LIAYAGTIAY ESMGLKTFGF AFGREDIWHP
EKDIYWGAEK DWLLPTDNDN SRYSGERNLE NPLAAVMMGL IYVNPEGVDG KPDPLKTAQD
IRETFARMAM NDEETVALTA GGHTVGKAHG NGNADLLGPE PEDADIHDQG FGWLNKAKRG
IGRDTVTSGI EGAWTTHPTQ WDNGYFTMLL NHEWELCKSP AGAWQWQPIN IKEEDKPRDV
EDPSISTMPM MTDADMAMKM DPEYRKISEH FHRDPEYFSK VFSRAWFKLT HRDMGPKVRY
LGPDVPVEDL LWQDPVPTGP KDFNVAVVKK AIKETGLSIS DMVTTAWDSA RTFRGSDKRG
GANGARIRLA LQKQWAGNEP KRLASVLSVL EPIAASHGVS VADVIVLAGN LGIELAAKKA
GFDVTVPFIS GRGDATDEMT DNESFAVLEP LHDGYRNWLK QDFAVSAEEL MLDRTQLMGL
TAHEMTVLVG GMRVIGTNYA ETGHGVFTER KGALTNDFFV NLTDMNYIWK PIGQNEYEIC
ERETGKRKWT ASRVDLIFGS NSVLRSYAEV YAQDDNKQKF VNDFISAWTK MMNADRFDVS
