KATG2_ECO57
ID KATG2_ECO57 Reviewed; 736 AA.
AC Q7BSW8; P77038;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Flags: Precursor;
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katP;
GN OrderedLocusNames=L7017, ECO57PM75;
OS Escherichia coli O157:H7.
OG Plasmid pO157.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; PLASMID=pO157;
RX PubMed=8969527; DOI=10.1099/13500872-142-11-3305;
RA Brunder W., Schmidt H., Karch H.;
RT "KatP, a novel catalase-peroxidase encoded by the large plasmid of
RT enterohaemorrhagic Escherichia coli O157:H7.";
RL Microbiology 142:3305-3315(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; PLASMID=pO157;
RX PubMed=9722640; DOI=10.1093/nar/26.18.4196;
RA Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J.,
RA Blattner F.R.;
RT "The complete DNA sequence and analysis of the large virulence plasmid of
RT Escherichia coli O157:H7.";
RL Nucleic Acids Res. 26:4196-4204(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; PLASMID=pO157;
RX PubMed=9628576; DOI=10.1093/dnares/5.1.1;
RA Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C.,
RA Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G.,
RA Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.;
RT "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an
RT enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak.";
RL DNA Res. 5:1-9(1998).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:8969527}.
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8969527}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X89017; CAA61429.1; -; Genomic_DNA.
DR EMBL; AF074613; AAC70085.1; -; Genomic_DNA.
DR EMBL; AB011549; BAA31832.1; -; Genomic_DNA.
DR PIR; T00313; T00313.
DR RefSeq; WP_000592771.1; NZ_SEKS01000027.1.
DR RefSeq; YP_002756743.1; NC_012487.1.
DR AlphaFoldDB; Q7BSW8; -.
DR SMR; Q7BSW8; -.
DR STRING; 155864.EDL933_p0015; -.
DR PeroxiBase; 2386; EcoH7CP02_EDL933.
DR EnsemblBacteria; AAC70085; AAC70085; Z_L7017.
DR EnsemblBacteria; BAA31832; BAA31832; BAA31832.
DR KEGG; ece:Z_L7017; -.
DR PATRIC; fig|83334.175.peg.3529; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000000558; Plasmid pO157.
DR Proteomes; UP000002519; Plasmid pO157.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; Periplasm;
KW Peroxidase; Plasmid; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 24..736
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000354782"
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 736 AA; 81794 MW; F3EA593D3FDEDB8D CRC64;
MIKKTLPVLI LLALSGSFST AVAADKKETQ NFYYPETLDL TPLRLHSPES NPWGADFDYA
TRFQQLDMEA LKKDIKDLLT TSQDWWPADY GHYGPFFIRM AWHGAGTYRT YDGRGGASGG
QQRFEPLNSW PDNVNLDKAR RLLWPVKKKY GSSISWGDLM VLTGNVALES MGFKTLGFAG
GREDDWESDL VYWGPDNKPL ADNRDKNGKL QKPLAATQMG LIYVNPEGPG GKPDPLASAK
DIREAFSRMA MDDEETVALI AGGHTFGKAH GAASPEKCIG AGPDGAPVEE QGLGWKNKCG
TGNGKYTITS GLEGAWSTSP TQFTMQYLKN LYKYEWELHK SPAGAYQWKP KKAANIVQDA
HDPSVLHPLM MFTTDIALKV DPEYKKITTR FLNDPKAFEQ AFARAWFKLT HRDMGPAARY
LGNEVPAESF IWQDPLPAAD YTMIDGKDIK SLKEQVMDLG IPASELIKTA WASASTFRVT
DYRGGNNGAR IRLQPEINWE VNEPEKLKKV LASLTSLQRE FNKKQSDGKK VSLADLIVLS
GNAAIEDAAR KAGVELEIPF TPGRTDASQE QTDVASFSVL EPTADGFRNY YSKSRSHISP
VESLIDKASQ LDLTVPEMTA LLGGLRVMDI NTNNSSLGVF TDTPGVLDNK FFVNLLDMST
RWSKADKEDT YNGFDRKTGA LKWKASSVDL IFSSNPELRA VAEVYASDDA RNKFIHDFVK
SWNKVMNSDR FDLNNK
