ID A0A0S2DJK9_LYSEN Unreviewed; 726 AA.
AC A0A0S2DJK9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:QCW26928.1};
GN ORFNames=FE772_16085 {ECO:0000313|EMBL:QCW26928.1}, GLE_3243
GN {ECO:0000313|EMBL:ALN58589.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN58589.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN58589.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN58589.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCW26928.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW26928.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) 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}.
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DR EMBL; CP013140; ALN58589.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW26928.1; -; Genomic_DNA.
DR RefSeq; WP_057948149.1; NZ_CP040656.1.
DR AlphaFoldDB; A0A0S2DJK9; -.
DR STRING; 69.GLE_3243; -.
DR KEGG; lez:GLE_3243; -.
DR PATRIC; fig|69.6.peg.3196; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000308311; 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 CDD; cd00649; catalase_peroxidase_1; 1.
DR CDD; cd08200; catalase_peroxidase_2; 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; 1.
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:UP000061569}.
FT DOMAIN 125..420
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 255
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 214..240
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 91)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 726 AA; 78685 MW; 67DE61CAFEF57DDF CRC64;
MSKESKCPFN HAAGGGTSNR DWWPNQLNLK ILHQQAPATD PMDAGFDYAE AFKSLDLDAV
KKDLHALMTD SQDWWPADFG HYGPLFIRMA WHSAGTYRIF DGRGGAGAGQ QRFAPLNSWP
DNGNLDKARR LLWPIKQKYG NKISWADLLI LTGNVALESM GFKTFGFAGG RADVWEPEEG
VYWGAETEWL GDKRYSGDRV LENPLGAVQM GLIYVNPQGP NGNPDPIAAA RDIRETFARM
AMNDEETVAL IAGGHSFGKT HGAGPESHVG REPEGADLAD QGLGWASSFN SGKAGDAITS
GLEVTWTSTP TQWSNEFFAN LFGYEWELSK SPAGAHQWIA KDPAAANKIP HAHDPSKRQA
PTMLTTDLSL RFDPAYEKIS RRFFENPDQF ADAFARAWFK LTHRDMGPRV RYLGKEVPAE
ELIWQDPIPA VDHPLVDAGD IAALKAKILA SGLSVSELVS TAWASASTFR GSDKRGGANG
ARIRLAPQKD WEVNQPAQLA KVLATLEGIQ KDFNAAAGGK KVSLADLIVL GGAAGVEQAA
KNAGVAIDVP FAPGRMDASA EQTDVESFAA LEPLADGFRN YLAGAYKPTA EALLIDRAQL
LDLSAPETAV LIGGLRVLGA NAGGSQHGVF TDKVGALSND FFVNLLDMGT VWKPTSDAQD
AFEGRDRKTG APKWTATRVD LVFGSHSQLR AIAEVYASGD AKEKFVRDFV AAWNKVMNAD
RFDLKK
//
