KATG_YERPS
ID KATG_YERPS Reviewed; 737 AA.
AC Q66E82;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=YPTB0811;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20051.1; -; Genomic_DNA.
DR RefSeq; WP_002209433.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66E82; -.
DR SMR; Q66E82; -.
DR PeroxiBase; 2639; YpsCP01.
DR EnsemblBacteria; CAH20051; CAH20051; YPTB0811.
DR GeneID; 66842768; -.
DR KEGG; ypo:BZ17_1745; -.
DR KEGG; yps:YPTB0811; -.
DR PATRIC; fig|273123.14.peg.1846; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000001011; 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 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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 24..737
FT /note="Catalase-peroxidase"
FT /id="PRO_5000098474"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 264
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 99
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 102..223
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 249)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 223..249
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 102)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 737 AA; 81365 MW; DB870BC41ABD469A CRC64;
MLKKILPVLI TLAIVHNTPT AWAAEAPKTD SFYLPKSLDL SPLRLHNIES NPYGKDFNYA
QQFKTLDLEA VKKDIKTVLT TSQDWWPADY GNYGPFFIRM AWHGAGTYRI YDGRGGADGG
QQRFEPLNSW PDNANLDKAR RLLWPIKKKY GAKISWGDLM VLTGNVALES MGFKTLGFAG
GREDDWQSDL VYWGAGNKML SDNRDKNGKL PKPLAATQMG LIYVNPEGPN GKPDPVAAAK
DIREAFARMA MNDEETVALI AGGHTFGKAH GAASPEKCLG AAPGEAGLEQ QGLGWANKCG
SGNGKDTITS GLEGAWTTDP THFTMQYLSN LYKHEWVLTK SPAGAWQWKP KNAANVVPDA
TDPTKFHPLM MFTTDIALKV DPEYKKITTR FLENPEEFKM AFARAWFKLT HRDMGPAARY
LGDEVPKETF IWQDPLPAAN YKMIDSADIS ELKDKILKTG LSDTKLIKTA WASASTFRGT
DFRGGDNGAR IRLAPQKDWP VNDPAELHSV LAALMEVQNN FNKDRSDGKK VSLSDLIVLG
GNAAIEDAAK KAGYSISIPF TPGRTDASQE ETDVSSFAVL EPTADGFRNY YDAKRNTLSP
IASLIDRANK LELTVPEMTV LIGGLRVLDV NSGGSKAGVL TNTPGQLNNN FFVNLLDMST
KWTKSPKAEG YFDGYDRKTG KLKWTASSVD LVFGSNPELR AVAEVYASDD AKEKFVHDFT
KVWEKVMNLD RFDIKNN
