ID A0A0A2WP17_9GAMM Unreviewed; 722 AA.
AC A0A0A2WP17;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN ORFNames=LF41_2192 {ECO:0000313|EMBL:KGQ20025.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ20025.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ20025.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ20025.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
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:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000256|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01961,
CC ECO:0000256|RuleBase:RU003451}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ20025.1}.
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DR EMBL; JRKJ01000004; KGQ20025.1; -; Genomic_DNA.
DR RefSeq; WP_036166306.1; NZ_JRKJ01000004.1.
DR AlphaFoldDB; A0A0A2WP17; -.
DR STRING; 1300345.LF41_2192; -.
DR PATRIC; fig|1300345.3.peg.772; -.
DR eggNOG; COG0376; Bacteria.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000030518; Unassembled WGS sequence.
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 CDD; cd00649; catalase_peroxidase_1; 1.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
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 NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 2.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_01961}; Reference proteome {ECO:0000313|Proteomes:UP000030518}.
FT DOMAIN 97..412
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 495..711
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 252
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:0000256|HAMAP-Rule:MF_01961"
FT SITE 86
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 211..237
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 89)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 722 AA; 79531 MW; FFB172DB8EC32902 CRC64;
MNEMSKCPVM AHRKTRNNSH WWPDQLNLDV LHQAKLSDPN LEDFDYKAEF KTLDLDAVVK
DLNDLMTDSQ DWWPADYGHY GPFFIRMAWH AAGTYRIFDG RGGARSGEQR FAPLNSWPDN
GNLDKARRLL WPIKQKYGRK LSWADLMILA GNVAIQSMGG PIFGFGGGRE DVWEPQPIDW
GPESTWLGDE RYSGDRELAN PFGAVQMGLI YVNPQGPNGN PDPVASGRDI RETFARMAMN
DYETVALVAG GHTFGKCHGA GPDSHVGNDP EGANIEELGF GWKSTFESGI AEHAITSGLE
GAWTATPTKW DMSYFETLFG NEWELTKSPA GAHQWKPKGD ANRNVPDAHV KGKVHQPMMT
TADLAMRFDP AYEKISRHFL ANPAEFADAF ARAWFKLTHR DMGPKIRYLG KLVPKEDLIW
QDPLPKAESS SIGEADIASL KKQILDSGLT IPQLVKAAWA SASTFRGTDL RGGANGARVR
LEPQKNFEAN EPAELDKVLS KLDSIRSASG KKISLADLIV LGGSAAVEAA AQKAGHAVTV
PFTPGRSDAT AEQTDADSFL VLEPALDGFR NYVRKGAEKL AAIALIDRAA LLTLTAPEMT
ALVGGMRALG ANTGNTKHGQ FTDRVGTLTT DFFHNLLDMR TAWKPSDKEP GVFEGTDRRS
GALKWTATMS DLIFGSNSQL RALAEVYAAS DGEKHFVQDF IAAWTKVMEL DRFDLKYRQE
AL
//
