KATG_DECAR
ID KATG_DECAR Reviewed; 736 AA.
AC Q479B7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Daro_3836;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ48564.1; -; Genomic_DNA.
DR RefSeq; WP_011289559.1; NC_007298.1.
DR AlphaFoldDB; Q479B7; -.
DR SMR; Q479B7; -.
DR STRING; 159087.Daro_3836; -.
DR PeroxiBase; 2367; DarCP01_RCB.
DR EnsemblBacteria; AAZ48564; AAZ48564; Daro_3836.
DR KEGG; dar:Daro_3836; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
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..736
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354766"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 265
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 96..224
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 250)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 224..250
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 736 AA; 80014 MW; 7D3C0F3432884025 CRC64;
MSNEQKCPFS GTHGARTTVG TQSNRDWWPK VLNLNILHQH APAANPMDAD FDYSETFKTL
DFGALKQDLY ALMTTSQDWW PADWGHYGGL FIRMAWHSAG TYRTGDGRGG AGTGNQRFAP
INSWPDNGNL DKARRLLWPI KQKYGNKISW ADLMILAGNC ALESMGFKTF GFGGGRVDIW
QPEEDIYWGA EREWLATSDK PNSRYSGERN LDNPLAAVQM GLIYVNPEGP DGNPDPVASG
RDIRETFARM AMNDEETVAL TAGGHTFGKA HGAGDPALVG PEPEAAPIEE QGLGWINKFG
SGKGIHATTS GIEGAWKPNP TKWDNGYFDM LFGYEWELTR SPAGAKQWVA KDCKPEHLIP
DAHDPSKKHP PMMTTADLAM RFDPIYGPIS RRFHQDPAAF ADAFARAWFK LTHRDLGPKA
RYLGPEVPAE DLVWQDPIPA VDHPLIEVTD VASLKAKLLA SGLSTAELVS TAWASASTFR
GSDKRGGANG ARIRLAPQKD WAANQPAQLA KVLGVLEGIQ QAFNSAQTGG KKVSLADLIV
LGGCAAVEAA AKAAGFAVAV PFTPGRTDAS QEQTDAESIA VLEPEADGFR NYQKKTYSVS
AEEMLVDKAQ LLTLSAPEMT VLVGGLRVLG GNVGGSSDGV FTTTPGTLSN DFFVNLLDMG
TVWKPAAESA GRYEGRDRQT GVAKWTASRV DLIFGSNSQL RALAEVYAQN DAQEKFVRDF
IAAWSKVMEL DRFDLK
