KATG_LEPBA
ID KATG_LEPBA Reviewed; 741 AA.
AC B0SD19;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=LBF_2421;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / Ames;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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; CP000777; ABZ94911.1; -; Genomic_DNA.
DR RefSeq; WP_012389443.1; NC_010842.1.
DR AlphaFoldDB; B0SD19; -.
DR SMR; B0SD19; -.
DR KEGG; lbf:LBF_2421; -.
DR HOGENOM; CLU_025424_2_0_12; -.
DR OMA; MILAGNC; -.
DR BioCyc; LBIF355278:LBF_RS12330-MON; -.
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;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 22..741
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354824"
FT ACT_SITE 110
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 106
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 109..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 109)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 741 AA; 82737 MW; 74E8023F67322DC4 CRC64;
MRNFRRFTIA LLVLFLGPIG AADTKETPGM DRQNTSNQFW WPERLDLAPL RQHGSESNPL
GRQFHYAKEF KELDIQTLKE EIKTVMKTSQ DWWPADYGHY GPFFIRMAWH SAGTYRISDG
RGGAGGGQQR FEPLNSWPDN ANLDKARRLL WPIKKKYGKK ISWADLMVLT GNVALESMGF
KTYGFAGGRT DDWEADLVYW GPEKKFLEDQ RYKGNRELKN PLAAVQMGLI YVNPEGPNGN
PDPLAAAKDI RETFGRMAMN DEETVALIAG GHTFGKAHGK SDPSKHVGKE PAAAGLEEQG
FGWKNNYKKG NAEDTITSGL EGAWTANPTK WTTQYLNNLF GFEWVQTKSP AGAIQWVPKD
GAGANMVPDA HDKSLRHAPI MFTTDLALKF DPSYKVIAKR FQENPKEFEL AFAKAWFKLT
HRDMGPLTRY IGKDLPKEPL IWQDPVPAVN HKLVGPKEIE SLKGKILKSG LSVPQLVRTA
WASAASFRST DMRGGANGAR IRLSPQKNWP VNDPDELSKV LKKLEQIQEE FNKSGNKISL
ADLIVLAGNA AIEEAAKKAG VKVTVPFTPG RTDATIEQTD EYSFSVLEPK ADAFRNYYGP
GNLMSPTEML VDRANMLSLS IPEMTVLLGG MRSLDANAGK SKHGILTTKP GVLSNDFFVN
LLDMSTKWQK SEQTEGLYEG LDRKTGSKRW TATSVDLIFG SHSELRAVAE VYASDDAKEK
FVKDFVSAWN KVMMLDRFDV K
