KATG_PSEPG
ID KATG_PSEPG Reviewed; 751 AA.
AC B0KNK9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=PputGB1_2231;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-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; CP000926; ABY98132.1; -; Genomic_DNA.
DR RefSeq; WP_012271880.1; NC_010322.1.
DR AlphaFoldDB; B0KNK9; -.
DR SMR; B0KNK9; -.
DR STRING; 76869.PputGB1_2231; -.
DR EnsemblBacteria; ABY98132; ABY98132; PputGB1_2231.
DR KEGG; ppg:PputGB1_2231; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000002157; 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..751
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354867"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 285
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 87
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 90..244
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 270)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 244..270
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 90)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 751 AA; 81701 MW; E5A0847D7F19520A CRC64;
MSNESKCPFH QTAGGGTTNR DWWPDQLNLR ILHQHSSKSS PDPDFDYAKA FKSLDFQALK
KDLTALMTDS QDWWPADFGH YGPLFIRMAW HSAGTYRIGD GRGGAGSGQQ RFAPLNSWPD
NVSLDKARRL LWPIKQKYGN KISWADLIVL TGNVALESMG FKTFGFSGGR ADVWEPDEDV
YWGSEKVWLG GDTRYGKDQL KAQAPGQGDL VAEPAKHGEE QNRDLSAERN LENPLAAVQM
GLIYVNPEGP EGNPDPVASG KDIRETFGRM AMNDEETVAL IAGGHAFGKT HGAGPADNVG
PEPEAAGLEL QGLGWANKFG TGKGGDAITS GLEVIWTSTP TKWSNEYLNN LFNFEWELTK
SPAGAHQWRP KEGKGAGTVP DAHDPGKKHA PSMLTSDLAL RFDPIYEPIA RRFKDNPDQL
ADAFARAWYK LIHRDMGPLA RYLGPEMPNE ELLWQDPLPK ADPSTIGEQD IAALKAKVLA
SGLSVGELVS TAWASASTFR GSDKRGGANG ARLRLAPQKG WAANQGVDKV LAALEKIQGE
FNNGGKKISL ADLIVLAGTA AVEKAAKDAG YSGSVGFRPG RVDASEAQTD VESFAVLEPL
ADGFRNFSKA RYSVKAEKLL LDKAQLLTLT APELTVLVGG LRVLGANHGG SKLGVFTDKP
GTLSNDFFRN LLDMSVEWKP TSADNETFEG RDRKTGQVKW SGSRVDLVFG SHAQLRALSE
VYGSSDGADK FVRDFVAAWQ KVMELDRFDL K
