KATG_SHESW
ID KATG_SHESW Reviewed; 728 AA.
AC A1REM5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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};
GN OrderedLocusNames=Sputw3181_0269;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-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; CP000503; ABM23120.1; -; Genomic_DNA.
DR RefSeq; WP_011787666.1; NC_008750.1.
DR AlphaFoldDB; A1REM5; -.
DR SMR; A1REM5; -.
DR PeroxiBase; 3623; SHspCP01_W3-18-1.
DR GeneID; 45040844; -.
DR KEGG; shw:Sputw3181_0269; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000002597; 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.
FT CHAIN 1..728
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354927"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 266
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 94
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 97..225
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 251)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 225..251
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 97)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 728 AA; 81303 MW; D34F34094D910084 CRC64;
MDKTHSSQGK CPVMHGGNTS VTTNNMDWWP KALNLDILHQ HDKKTDPMDP TFNYSEAFKT
LDLAAVKQDL YALMTDSQDW WPADWGHYGG LMIRMAWHSA GTYRIADGRG GAGTGNQRFA
PLNSWPDNAN LDKARRLLWP IKKKYGNKLS WADLIILAGN VAYESMGLKT YGFAGGRADI
WHPEKDIYWG SEKQWLAPSD NPNSRYSGER DLENPLAAVM MGLIYVNPEG VDGNPDPLRT
AQDIRITFAR MAMDDEETVA LTAGGHTVGK CHGNGKAQNL GPEPEAEDVE AQGLGWLNKH
GRGVGRNTVT SGIEGAWTTH PTQWDNGYFS LLLGYDWELK KSPAGAWQWE PINIKEEDKP
VDVEDPTIRH NPIMTDADMA MKMDPEYRKI SEKFYKDPAY FSEVFARAWF KLTHRDLGPK
SRYLGPEVPA EDLIWQDPIP QVDYRLSDDD ITALKAKILA SGLSIAELVT TAWDSARTFR
GSDYRGGANG ARIRLAPQKD WEGNEPVRLQ KVLKVLTDIQ TGLSQKVSIA DLIVLGGTAA
VEKAAQDAGV NIRVPFASGR GDASQEMTDI ESFAVLEPLH DAYRNWQKKD YVVQPEELML
DRTQLMGLTA HEMTVLIGGM RVLGANYAGS AHGVFTDRVG VLSNDFFVNL TDMSYNWKPA
GNNLYQIIER KTGTVKWTAT RVDLVFGSNS VLRSYAEIYA QDDAKEKFVH DFVNAWTKVM
NADRFDLA
