KATG_JANMA
ID KATG_JANMA Reviewed; 725 AA.
AC A6SY97;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-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=mma_1554;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88756.1; -; Genomic_DNA.
DR RefSeq; WP_012079409.1; NC_009659.1.
DR AlphaFoldDB; A6SY97; -.
DR SMR; A6SY97; -.
DR STRING; 375286.mma_1554; -.
DR PRIDE; A6SY97; -.
DR EnsemblBacteria; ABR88756; ABR88756; mma_1554.
DR KEGG; mms:mma_1554; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR BioCyc; JSP375286:MMA_RS08095-MON; -.
DR Proteomes; UP000006388; 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 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; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..725
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354813"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 256
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..215
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 241)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 215..241
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 725 AA; 79946 MW; 8143CC753706B446 CRC64;
MSSEAKCPFP HAANRSRSNQ DWWPNQLRVD VLNQHSNKSN PLGEKFNYAE EFKKLDYKAL
KADLVKLMTD SQDWWPADFG HYGPQFVRMA WHATGTYRTM DGRGGGGRGQ QRFAPLNSWP
DNVNIDKSRR LLWPIKQKYG QRISWADLLV LTGNVALESM GFRTFGFAGG RADVWEPDTD
VNWGAETTWL GTDKRFSGDR ELDENLSATH MGLIYVNPEG PDGSGDYMAA AKDIRATFYR
MAMDDEEIVA LIAGGHTFGK AHGAAPESHK GAEPEGAPIE AQGLGWVSNF GDGYGKDTVS
SGLEVTWTKT PALWSNNFFE NLFKYEWEIT KSPAGAKQWV AKDAEDIIPD AHIKGKFHKP
TMLTTDLTLR FDPEFGKISK RFYEDPQAFA EAFARAWFKL THRDMGPRSR YLGPEVPKEE
LIWQDPIPEV DYKLVDAADV TALKAKLLTS GLSVSELVGT AWASASTFRG SDKRGGANGA
RIRLAPMKDW EVNQPEQLAK VLKTLEGIQA DFNQSASGGK QVSLADLIVL AGSVGVEQAA
KAAGVNVSVP FAAGRNDARQ DQTDVESFAA LEPRTDGFRN YVGKKNGVPA EVALIDKAQL
LCLSVPELTV LISGLRAINI NVGGVKHGVL TRTPGVLNNE VLLNLLDMGT QWKPVESDAN
VFEGRDRKSG EVKWTATRAD LVFGSNSILR SVAEVYAESD AKEKFVKDFV AAWVKVMNAD
RFDLA
