KATG_FRASN
ID KATG_FRASN Reviewed; 743 AA.
AC A8LBC6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Franean1_1533;
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC unclassified Frankia.
OX NCBI_TaxID=298653;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EAN1pec;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(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; CP000820; ABW10973.1; -; Genomic_DNA.
DR RefSeq; WP_020459147.1; NC_009921.1.
DR AlphaFoldDB; A8LBC6; -.
DR SMR; A8LBC6; -.
DR STRING; 298653.Franean1_1533; -.
DR PeroxiBase; 2353; FspCP_EAN1pec.
DR EnsemblBacteria; ABW10973; ABW10973; Franean1_1533.
DR KEGG; fre:Franean1_1533; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
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 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..743
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354798"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 272
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 105
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 108..231
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 257)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 231..257
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 108)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 743 AA; 80421 MW; 46AE1825592C563C CRC64;
MSENHETVVS ELNEESGGGC PVAHERAPHP TQGGGNRGWW PNRLNLKILA KNPAVANPLG
EEFDYAAAFR TLDLPAVKRD IAQVLTTSQD WWPADYGHYG PFMIRMAWHS AGTYRISDGR
GGGGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQAL SWADLMILAG NVALESMGFT
TFGFAGGRED VWEPDEDVYW GPETTWLGDE RYTGDRELEN PLGAVQMGLI YVNPEGPNGT
PDPLAAARDI RETFRRMAMD DEETVALIAG GHTFGKTHGA GDPDNVGPEP EGAPLETQGL
GWKNAFGTGK GADAITSGLE GAWTPTPVSW DNSFFETLFG YEWALTKSPA GAYQWKPKGG
AGAGTVPDAH DAAKSHAPTM LTTDLALRFD PVYEPISRRF LEHPDELADA FARAWFKLTH
RDMGPVARYL GPEVPAETLL WQDPVPAVDH ELVDAADVAA LKVRVLASGL SVSELVATAW
ASASTFRGGD KRGGANGARI RLEPQRGWEV NEPDRLAAVL GTLTGIQEEF HAARTDGRRV
SLADLIVLAG GAAVEQAARE AGFDVEVPFT PGRTDASQEL TDVESFAALE PAADGFRNYL
GKGQRLPAEY LLLDRANLLT LSAPELTVLV GGLRVLGANF RQSSLGVLTA TPGVLTNDFF
ANLLDLGTTW RPSGEDDNVF EGRDAATGEL TWTGSRVDLV FGSNSELRAF AEVYASDDAR
EKFVRDFVAA WAKVMNLDRY DLA
