KATG_XYLFM
ID KATG_XYLFM Reviewed; 757 AA.
AC B0U3C6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN OrderedLocusNames=Xfasm12_1432;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA12355.1; -; Genomic_DNA.
DR AlphaFoldDB; B0U3C6; -.
DR SMR; B0U3C6; -.
DR KEGG; xfm:Xfasm12_1432; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
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.
FT CHAIN 1..757
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354960"
FT REGION 210..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 289
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 98
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 101..248
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 274)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 248..274
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 101)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 757 AA; 83696 MW; FF3F0016FE1146F2 CRC64;
MRDMRASSPE TTSAVKCPFN KTAVEGTHNK DWWPNQLRVD LLHQHSNKSN PLGETFDYAK
VFQKLDYAAL KRDLHALMTD SQDWWPADFG HYGGLFIRMA WHSAGTYRIG DGRGGAGRGQ
QRFAPLNSWP DNVSLDKARR LLWPIKKKYG QQISWADLIV LAGNVALESM GFKTFGFAGG
RVDTWEPDQD VYWGREMTWL GGDVRYGAVS EGVHHPDEHS GAKEKASKNS DSRVLENPLA
AVQMGLIYVN PEGPDGRPDP LASARDIRET FARMAMNDEE TVALIAGGHT FGKTHGAAPA
DNVGPEPEAG ELEQQGLGWH NRFGSGKAGD TITSGLEVTW TKTPTQWSND FFEHLFGYEW
ELTKSPAGAY QWVAKDAAAT IPHAHDPSKK LLPMMLTSDL ALRFDPVYEK ISRHFHAHPD
QFADAFARAW FKLTHRDMGP RVRYLGPEVP AEELIWQDPV PKVSHVLVDA QDLLALKHKI
SASGLGISQL VSTAWASAST FRGSDKRGGA NGGRLCLAPQ NQWEVNQPQQ LSVVLETLRR
VQTEFNAQAG DKRISLADLI VLAGGVGVEQ AAKRVGIVVE VPFVPGRTDA LQEQTDVSSF
APLEPFADGF RNYVKGDEVV PSEHLLIDRA QLLTLTAPEM TVLIGGLRVL GANVGGVKHG
VFTDRLGTLS NDFFINLLDM GTEWAPVSKE RHVFEGRDRR TGVLKWTGTR VDLVFGSNAL
LRALAEVYAA VDAQEKFVRD FVAAWSKVMH LDRFDLV
