KATG_ECOLI
ID KATG_ECOLI Reviewed; 726 AA.
AC P13029; Q2M8N8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 192.
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=Hydroperoxidase I {ECO:0000303|PubMed:374409};
DE Short=HPI {ECO:0000303|PubMed:374409};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=b3942, JW3914;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3045098; DOI=10.1128/jb.170.9.4415-4419.1988;
RA Triggs-Raine B.L., Doble B.W., Mulvey M.R., Sorby P.A., Loewen P.C.;
RT "Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli.";
RL J. Bacteriol. 170:4415-4419(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-339.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 309-726.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, HEME-BINDING, AND
RP COFACTOR.
RX PubMed=374409; DOI=10.1016/s0021-9258(18)50722-5;
RA Claiborne A., Fridovich I.;
RT "Purification of the o-dianisidine peroxidase from Escherichia coli B.";
RL J. Biol. Chem. 254:4245-4252(1979).
RN [7]
RP COVALENT BOND.
RX PubMed=12832453; DOI=10.1074/jbc.m304053200;
RA Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T.,
RA Singh R., Switala J., Carpena X., Fita I., Loewen P.C.;
RT "Characterization of the catalase-peroxidase KatG from Burkholderia
RT pseudomallei by mass spectrometry.";
RL J. Biol. Chem. 278:35687-35692(2003).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
RA Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
RT "Comparative study of catalase-peroxidases (KatGs).";
RL Arch. Biochem. Biophys. 471:207-214(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23416055; DOI=10.1016/j.celrep.2013.01.026;
RA Dorsey-Oresto A., Lu T., Mosel M., Wang X., Salz T., Drlica K., Zhao X.;
RT "YihE kinase is a central regulator of programmed cell death in bacteria.";
RL Cell Rep. 3:528-537(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 422-726.
RX PubMed=15388929; DOI=10.1107/s0907444904020621;
RA Carpena X., Melik-Adamyan W., Loewen P.C., Fita I.;
RT "Structure of the C-terminal domain of the catalase-peroxidase KatG from
RT Escherichia coli.";
RL Acta Crystallogr. D 60:1824-1832(2004).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Also displays NADH oxidase, INH lyase and
CC isonicotinoyl-NAD synthase activities. {ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:23416055, ECO:0000269|PubMed:374409}.
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:0000269|PubMed:374409};
CC Note=Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.
CC {ECO:0000269|PubMed:374409};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC KM=4.2 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC KM=3.9 mM for H(2)O(2) for the catalase reaction (at pH 7.5)
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC KM=60 uM for H(2)O(2) for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC KM=24 uM for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC Vmax=3730 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:374409};
CC Vmax=2220 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 7.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC Vmax=18 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409};
CC pH dependence:
CC Optimum pH is 4.25 for the peroxidase reaction and 7.5 for the
CC catalase reaction. {ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:374409};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:374409}.
CC -!- INDUCTION: By hydrogen peroxide.
CC -!- PTM: The N-terminus is blocked.
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 -!- DISRUPTION PHENOTYPE: Cells are more sensitive to killing by nalidixic
CC acid, the effect is mitigated by pretreatment with 2,2'-bipyridyl and
CC thiourea, both of which inhibit hydroxyl radical accumulation.
CC {ECO:0000269|PubMed:23416055}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; M21516; AAA24040.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76924.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77368.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03074.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43048.1; -; Genomic_DNA.
DR PIR; A65201; CSECHP.
DR RefSeq; NP_418377.1; NC_000913.3.
DR RefSeq; WP_001295695.1; NZ_SSZK01000014.1.
DR PDB; 1U2J; X-ray; 2.30 A; A/B/C/D/E/F/G/H=422-726.
DR PDB; 1U2K; X-ray; 2.00 A; A=422-726.
DR PDB; 1U2L; X-ray; 2.30 A; A/B=422-726.
DR PDBsum; 1U2J; -.
DR PDBsum; 1U2K; -.
DR PDBsum; 1U2L; -.
DR AlphaFoldDB; P13029; -.
DR SMR; P13029; -.
DR BioGRID; 4263062; 16.
DR DIP; DIP-10053N; -.
DR IntAct; P13029; 12.
DR MINT; P13029; -.
DR STRING; 511145.b3942; -.
DR PeroxiBase; 2394; EcoCP01_K-12.
DR SWISS-2DPAGE; P13029; -.
DR jPOST; P13029; -.
DR PaxDb; P13029; -.
DR PRIDE; P13029; -.
DR EnsemblBacteria; AAC76924; AAC76924; b3942.
DR EnsemblBacteria; BAE77368; BAE77368; BAE77368.
DR GeneID; 948431; -.
DR KEGG; ecj:JW3914; -.
DR KEGG; eco:b3942; -.
DR PATRIC; fig|511145.12.peg.4063; -.
DR EchoBASE; EB0506; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR InParanoid; P13029; -.
DR OMA; MILAGNC; -.
DR PhylomeDB; P13029; -.
DR BioCyc; EcoCyc:HYDROPEROXIDI-MON; -.
DR BioCyc; MetaCyc:HYDROPEROXIDI-MON; -.
DR SABIO-RK; P13029; -.
DR EvolutionaryTrace; P13029; -.
DR PRO; PR:P13029; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004096; F:catalase activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0004601; F:peroxidase activity; IDA:EcoCyc.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:EcoCyc.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IEP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..726
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055564"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 267
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 SITE 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 105..226
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 252)"
FT /evidence="ECO:0000269|PubMed:12832453"
FT CROSSLNK 226..252
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 105)"
FT /evidence="ECO:0000305|PubMed:12832453"
FT CONFLICT 621
FT /note="A -> G (in Ref. 1; AAA24040)"
FT /evidence="ECO:0000305"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:1U2L"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:1U2K"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:1U2L"
FT HELIX 464..475
FT /evidence="ECO:0007829|PDB:1U2K"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:1U2J"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 506..520
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 525..543
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 566..570
FT /evidence="ECO:0007829|PDB:1U2K"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1U2K"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 591..601
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 606..619
FT /evidence="ECO:0007829|PDB:1U2K"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1U2J"
FT HELIX 641..647
FT /evidence="ECO:0007829|PDB:1U2K"
FT STRAND 651..657
FT /evidence="ECO:0007829|PDB:1U2K"
FT STRAND 662..667
FT /evidence="ECO:0007829|PDB:1U2K"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:1U2K"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 688..697
FT /evidence="ECO:0007829|PDB:1U2K"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:1U2K"
FT HELIX 703..718
FT /evidence="ECO:0007829|PDB:1U2K"
FT TURN 719..721
FT /evidence="ECO:0007829|PDB:1U2K"
SQ SEQUENCE 726 AA; 80024 MW; 24D32EBED5DE9BD6 CRC64;
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF
DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA
GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG
FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS
AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP
DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS
RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG
GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA
ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK
ELFEGRDRET GEVKFTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL
DRFDLL
