KATG_PSEU5
ID KATG_PSEU5 Reviewed; 743 AA.
AC A4VK13;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=PST_1629;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP79314.1; -; Genomic_DNA.
DR RefSeq; WP_011912791.1; NC_009434.1.
DR AlphaFoldDB; A4VK13; -.
DR SMR; A4VK13; -.
DR STRING; 379731.PST_1629; -.
DR EnsemblBacteria; ABP79314; ABP79314; PST_1629.
DR KEGG; psa:PST_1629; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; KWTATRM; -.
DR Proteomes; UP000000233; 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;
KW Reference proteome.
FT CHAIN 1..743
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354870"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
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 97
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 100..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 100)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 743 AA; 81903 MW; 907DF5667F2A4B4E CRC64;
MNAESGENAG GGCPLGHGAG APRKRPSNRD WWPEALSLTS LNQHSPRSNP YGGDFDYAAE
FNSLDLDAVI ADLHKVMTDS QDWWPADFGH YGGLFIRMAW HSAGTYRITD GRGGAGGGQQ
RFAPLNSWPD NASLDKARRL LWPIKQKYGR KLSWADLFVL TGNVALESMG FKTFGFGGGR
ADTWEPEELF WGPEGTWLGD ERYSGERQLH PGLGAVQMGL IYVNPEGPNG NPDPKAAAVD
IRETFARMAM NDYETVALIA GGHTFGKTHG AGDPSFIGPE PEGALIEDQG LGWRSKFQTG
IGPDAITSGL EVIWSQTPVK WSNYFFENLF NFEWELTKSP AGAHQWVAKD APEIIPDPFD
PNKKRKPTML TTDLSLRFDP IYEPISRHFL ENPDEFADAF ARAWFKLTHR DMGPIARYLG
PLVPKEQLIW QDPIPERDHP VIDDADIASL KQKILGLGFS VSDLVSVAWA SAATYRGSDK
RGGANGARIR FAPQKDWEIN NPPLLAQVLQ KLGEIQSDFN GSATGGKKVS MADLIVLAGC
AAIEKAAQDG GVNVAVPFTP GRMDALEEWT DAQSFEALRP VADGFRNYYH ESHFMAPEEA
LVDKAHLLRL SAPEMTVLVG GMRVLGANAG GSQDGVFTHR VGVLSNDFFV NLLDMKNEWT
ATEHKNRFQG LDRKTRQPTW TATRVDLIFG SQSELRAQAE VYGMADGNEK FVRDFAKAWD
KVMNADRMDI GKPADQFSQK LSA
