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Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)

 KATG_MYCTU              Reviewed;         740 AA.
P9WIE5; J9VFD2; O08221; Q08129; Q50544; Q50546; Q50551; Q50552;
Q50553; Q50554; Q50555; Q50762; Q57215; Q57274;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
20-JUN-2018, entry version 37.
RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000303|PubMed:8320241, ECO:0000303|PubMed:9006925};
Short=CP {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000303|PubMed:15231843};
EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9006925};
AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
Name=katG {ECO:0000303|PubMed:8320241}; OrderedLocusNames=Rv1908c;
ORFNames=MTCY180.10;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=8320241; DOI=10.1128/jb.175.13.4255-4259.1993;
Heym B., Zhang Y., Poulet S., Young D., Cole S.T.;
"Characterization of the katG gene encoding a catalase-peroxidase
required for the isoniazid susceptibility of Mycobacterium
tuberculosis.";
J. Bacteriol. 175:4255-4259(1993).
[2]
SEQUENCE REVISION.
Cole S.T.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=7798673; DOI=10.1093/infdis/171.1.240;
Cockerill F.R. III, Uhl J.R., Temesgen Z., Zhang Y., Stockman L.,
Roberts G.D., Williams D.L., Kline B.C.;
"Rapid identification of a point mutation of the Mycobacterium
tuberculosis catalase-peroxidase (katG) gene associated with isoniazid
resistance.";
J. Infect. Dis. 171:240-245(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=INH-resistant strains;
Marttila H.J., Soini H., Huovinen P., Viljanen M.K.;
"katG gene mutations in isoniazid-resistant Mycobacterium tuberculosis
strains isolated from Finnish patients.";
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=2937643, 3150565, 3264812, MTB001, MTB003, MTB005, and MTB007;
PubMed=22972833; DOI=10.1128/JCM.01893-12;
Daum L.T., Rodriguez J.D., Worthy S.A., Ismail N.A., Omar S.V.,
Dreyer A.W., Fourie P.B., Hoosen A.A., Chambers J.P., Fischer G.W.;
"Next-generation ion torrent sequencing of drug resistance mutations
in Mycobacterium tuberculosis strains.";
J. Clin. Microbiol. 50:3831-3837(2012).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN ISONIAZID
ACTIVATION, AND ISONIAZID RESISTANCE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=1501713; DOI=10.1038/358591a0;
Zhang Y., Heym B., Allen B., Young D., Cole S.T.;
"The catalase-peroxidase gene and isoniazid resistance of
Mycobacterium tuberculosis.";
Nature 358:591-593(1992).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
STRAIN=ATCC 25618 / H37Rv;
Song J., Deretic V.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-740, FUNCTION, AND DOMAIN.
STRAIN=ATCC 25618 / H37Rv;
PubMed=10463167; DOI=10.1099/13500872-145-8-2011;
Mulder M.A., Nair S., Abratt V.R., Zappe H., Steyn L.M.;
"Involvement of the N- and C-terminal domains of Mycobacterium
tuberculosis KatG in the protection of mutant Escherichia coli against
DNA-damaging agents.";
Microbiology 145:2011-2021(1999).
[10]
FUNCTION, AND INDUCTION.
PubMed=8658136; DOI=10.1126/science.272.5268.1641;
Sherman D.R., Mdluli K., Hickey M.J., Arain T.M., Morris S.L.,
Barry C.E. III, Stover C.K.;
"Compensatory ahpC gene expression in isoniazid-resistant
Mycobacterium tuberculosis.";
Science 272:1641-1643(1996).
[11]
FUNCTION AS A CATALASE-PEROXIDASE, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-463, AND SUBUNIT.
PubMed=9006925; DOI=10.1074/jbc.272.5.2834;
Johnsson K., Froland W.A., Schultz P.G.;
"Overexpression, purification, and characterization of the catalase-
peroxidase KatG from Mycobacterium tuberculosis.";
J. Biol. Chem. 272:2834-2840(1997).
[12]
FUNCTION AS A PEROXYNITRITASE.
PubMed=10080924; DOI=10.1006/bbrc.1999.0358;
Wengenack N.L., Jensen M.P., Rusnak F., Stern M.K.;
"Mycobacterium tuberculosis KatG is a peroxynitritase.";
Biochem. Biophys. Res. Commun. 256:485-487(1999).
[13]
INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11401695; DOI=10.1046/j.1365-2958.2001.02427.x;
Pym A.S., Domenech P., Honore N., Song J., Deretic V., Cole S.T.;
"Regulation of catalase-peroxidase (KatG) expression, isoniazid
sensitivity and virulence by furA of Mycobacterium tuberculosis.";
Mol. Microbiol. 40:879-889(2001).
[14]
FUNCTION IN PATHOGENESIS, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=15165233; DOI=10.1111/j.1365-2958.2004.04078.x;
Ng V.H., Cox J.S., Sousa A.O., MacMicking J.D., McKinney J.D.;
"Role of KatG catalase-peroxidase in mycobacterial pathogenesis:
countering the phagocyte oxidative burst.";
Mol. Microbiol. 52:1291-1302(2004).
[15]
MET-TYR-TRP CROSS-LINK.
PubMed=15840564; DOI=10.1074/jbc.M502486200;
Ghiladi R.A., Knudsen G.M., Medzihradszky K.F.,
Ortiz de Montellano P.R.;
"The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-
peroxidase (KatG): autocatalytic formation and effect on enzyme
catalysis and spectroscopic properties.";
J. Biol. Chem. 280:22651-22663(2005).
[16]
CATALYTIC MECHANISM.
PubMed=17260948; DOI=10.1021/bi062266+;
Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C.;
"Redox intermediates in the catalase cycle of catalase-peroxidases
from Synechocystis PCC 6803, Burkholderia pseudomallei, and
Mycobacterium tuberculosis.";
Biochemistry 46:1183-1193(2007).
[17]
RADICAL INTERMEDIATE, AND ACTIVE SITE.
PubMed=18052167; DOI=10.1021/ja075108u;
Singh R., Switala J., Loewen P.C., Ivancich A.;
"Two [Fe(IV)=O Trp*] intermediates in M.tuberculosis catalase-
peroxidase discriminated by multifrequency (9-285 GHz) EPR
spectroscopy: reactivity toward isoniazid.";
J. Am. Chem. Soc. 129:15954-15963(2007).
[18]
FUNCTION AS A CATALASE-PEROXIDASE, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
"Comparative study of catalase-peroxidases (KatGs).";
Arch. Biochem. Biophys. 471:207-214(2008).
[19]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[21]
DRUG RESISTANCE.
PubMed=21244531; DOI=10.1111/j.1365-2958.2011.07547.x;
Ando H., Kitao T., Miyoshi-Akiyama T., Kato S., Mori T., Kirikae T.;
"Downregulation of katG expression is associated with isoniazid
resistance in Mycobacterium tuberculosis.";
Mol. Microbiol. 79:1615-1628(2011).
[22]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 2-740 IN COMPLEX WITH HEME,
COFACTOR, TRP-TYR-MET CROSS-LINK, AND SUBUNIT.
PubMed=15231843; DOI=10.1074/jbc.M402382200;
Bertrand T., Eady N.A.J., Jones J.N., Jesmin X., Nagy J.M.,
Jamart-Gregoire B., Raven E.L., Brown K.A.;
"Crystal structure of Mycobacterium tuberculosis catalase-
peroxidase.";
J. Biol. Chem. 279:38991-38999(2004).
[23]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF WILD-TYPE AND MUTANT THR-315
IN COMPLEX WITH HEME, SUBUNIT, INH ACTIVATION, AND MUTAGENESIS OF
SER-315.
PubMed=16566587; DOI=10.1021/bi051967o;
Zhao X., Yu H., Yu S., Wang F., Sacchettini J.C., Magliozzo R.S.;
"Hydrogen peroxide-mediated isoniazid activation catalyzed by
Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T
mutant.";
Biochemistry 45:4131-4140(2006).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANTS SER-137 AND LEU-418
IN COMPLEX WITH HEME, FUNCTION IN INH ACTIVATION, BIOPHYSICOCHEMICAL
PROPERTIES, DRUG RESISTANCE, AND MUTAGENESIS OF ASP-137; TYR-229;
SER-315; TRP-321 AND ARG-418.
PubMed=24185282; DOI=10.1039/c3cc47022a;
Zhao X., Hersleth H.P., Zhu J., Andersson K.K., Magliozzo R.S.;
"Access channel residues Ser315 and Asp137 in Mycobacterium
tuberculosis catalase-peroxidase (KatG) control peroxidatic activation
of the pro-drug isoniazid.";
Chem. Commun. (Camb.) 49:11650-11652(2013).
-!- FUNCTION: Bifunctional enzyme with both catalase and broad-
spectrum peroxidase activity, oxidizing various electron donors
including NADP(H) (PubMed:9006925, PubMed:18178143). Protects
M.tuberculosis against toxic reactive oxygen species (ROS)
including hydrogen peroxide as well as organic peroxides and thus
contributes to its survival within host macrophages by countering
the phagocyte oxidative burst (PubMed:8658136, PubMed:15165233).
Also displays efficient peroxynitritase activity, which may help
the bacterium to persist in macrophages (PubMed:10080924).
{ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:10080924,
ECO:0000269|PubMed:15165233, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:8658136, ECO:0000269|PubMed:9006925}.
-!- FUNCTION: Might be involved in DNA repair. Partly complements
recA-deficient E.coli cells exposed to UV radiation, mitomycin C
or hydrogen peroxide. Increases resistance to mitomycin C in
E.coli cells deficient for either uvrA, uvrB or uvrC.
{ECO:0000269|PubMed:10463167}.
-!- FUNCTION: Catalyzes the oxidative activation of the antitubercular
pro-drug isoniazid (INH) to generate an isonicotinoyl radical that
then reacts nonenzymatically with NAD to form an isonicotinoyl-NAD
adduct which inhibits InhA. {ECO:0000269|PubMed:16566587,
ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:24185282,
ECO:0000269|PubMed:9006925, ECO:0000269|PubMed:9634230}.
-!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9006925}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9006925}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:15231843,
ECO:0000269|PubMed:9006925};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000269|PubMed:15231843,
ECO:0000269|PubMed:9006925};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.4 mM for H(2)O(2) in the catalase reaction (at pH 7.0)
{ECO:0000269|PubMed:18178143};
KM=225 mM for H(2)O(2) in the catalase reaction (at pH 5.5-6.0)
{ECO:0000269|PubMed:18178143};
KM=5.18 mM for H(2)O(2) in the catalase reaction (at pH 7.0 and
25 degrees Celsius) {ECO:0000269|PubMed:9006925};
KM=360 uM for H(2)O(2) in the peroxidase reaction
{ECO:0000269|PubMed:18178143};
KM=67 uM for ABTS {ECO:0000269|PubMed:18178143};
KM=192 uM for isoniazid (at pH 7.2)
{ECO:0000269|PubMed:24185282};
Vmax=7620 umol/min/mg enzyme for the catalase reaction (at pH
5.5-6.0) {ECO:0000269|PubMed:18178143};
Vmax=5700 umol/min/mg enzyme for the catalase reaction (at pH
7.0) {ECO:0000269|PubMed:18178143};
Vmax=14 umol/min/mg enzyme for the peroxidase reaction with ABTS
as substrate {ECO:0000269|PubMed:18178143};
Note=kcat is 10100 sec(-1) for the catalase reaction (at pH 7.0
and 25 degrees Celsius). {ECO:0000269|PubMed:9006925};
pH dependence:
Optimum pH is 7.0 for the catalase activity and 4.5-5.5 for the
peroxidase activity (PubMed:9006925). Optimum pH is 4.75 for the
peroxidase activity (PubMed:18178143).
{ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9006925};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15231843,
ECO:0000269|PubMed:16566587, ECO:0000269|PubMed:9006925}.
-!- INDUCTION: By treatment with H(2)O(2) (PubMed:8658136). Repressed
by FurA (PubMed:11401695). {ECO:0000269|PubMed:11401695,
ECO:0000269|PubMed:8658136}.
-!- DOMAIN: Consists of two related domains. The catalase-peroxidase
activity is associated with the N-terminal domain but no definite
function has been assigned to the C-terminal domain, although it
may play a role in substrate binding.
{ECO:0000305|PubMed:10463167}.
-!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is
important for the catalase, but not the peroxidase activity of the
enzyme (By similarity). The formation of the Trp-Tyr-Met cross-
link is autocatalytic (PubMed:15840564). {ECO:0000255|HAMAP-
Rule:MF_01961, ECO:0000269|PubMed:15840564}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are devoid of
catalase activity, supersensitive to H(2)O(2) exposure and highly
resistant to the antitubercular drug isoniazid (INH) in vitro.
This mutant strain is markedly attenuated for virulence in mice
and displays impaired growth in infected macrophages, but its
growth and survival is indistinguishable from wild-type in
macrophages lacking the ROS-generating NADPH oxidase (Phox).
{ECO:0000269|PubMed:15165233}.
-!- MISCELLANEOUS: In contrast to the Synechocystis sp. enzyme, no Trp
radical is formed on the distal Trp residue (Trp-91).
{ECO:0000269|PubMed:18052167}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
{ECO:0000305|PubMed:19099550}.
-!- MISCELLANEOUS: Many isoniazid-resistant clinical isolates contain
mutations in katG, leading to abolition or reduction of
catalase/peroxidase activity which results in lack of INH
activation, or to a reduced affinity for INH. Other mechanisms of
INH resistance include deletion of the katG gene, and down-
regulation of katG expression due to mutations in the furA-katG
intergenic region. {ECO:0000305, ECO:0000305|PubMed:1501713,
ECO:0000305|PubMed:21244531, ECO:0000305|PubMed:24185282}.
-!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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EMBL; X68081; CAA48213.1; -; Genomic_DNA.
EMBL; U06258; AAB04159.1; -; Unassigned_DNA.
EMBL; U40593; AAA85167.1; -; Genomic_DNA.
EMBL; U40595; AAA85169.1; -; Genomic_DNA.
EMBL; U41305; AAA85171.1; -; Genomic_DNA.
EMBL; U41306; AAA85172.1; -; Genomic_DNA.
EMBL; U41307; AAA85173.1; -; Genomic_DNA.
EMBL; U41308; AAA85174.1; -; Genomic_DNA.
EMBL; U41309; AAA85175.1; -; Genomic_DNA.
EMBL; U41310; AAA85176.1; -; Genomic_DNA.
EMBL; U41311; AAA85177.1; -; Genomic_DNA.
EMBL; U41312; AAA85178.1; -; Genomic_DNA.
EMBL; U41313; AAA85179.1; -; Genomic_DNA.
EMBL; U41314; AAA85180.1; -; Genomic_DNA.
EMBL; JX303265; AFR90354.1; -; Genomic_DNA.
EMBL; JX303270; AFR90359.1; -; Genomic_DNA.
EMBL; JX303273; AFR90362.1; -; Genomic_DNA.
EMBL; JX303276; AFR90365.1; -; Genomic_DNA.
EMBL; JX303277; AFR90366.1; -; Genomic_DNA.
EMBL; JX303278; AFR90367.1; -; Genomic_DNA.
EMBL; JX303280; AFR90369.1; -; Genomic_DNA.
EMBL; AL123456; CCP44675.1; -; Genomic_DNA.
EMBL; AF002194; AAB63371.1; -; Genomic_DNA.
EMBL; L14268; AAA72374.1; -; Genomic_DNA.
PIR; A70519; A40662.
RefSeq; NP_216424.1; NC_000962.3.
RefSeq; WP_003899075.1; NZ_KK339370.1.
PDB; 1SFZ; Model; -; A=1-740.
PDB; 1SJ2; X-ray; 2.41 A; A/B=2-740.
PDB; 2CCA; X-ray; 2.00 A; A/B=1-740.
PDB; 2CCD; X-ray; 2.10 A; A/B=1-740.
PDB; 4C50; X-ray; 2.50 A; A/B=1-740.
PDB; 4C51; X-ray; 3.10 A; A/B=1-740.
PDBsum; 1SFZ; -.
PDBsum; 1SJ2; -.
PDBsum; 2CCA; -.
PDBsum; 2CCD; -.
PDBsum; 4C50; -.
PDBsum; 4C51; -.
ProteinModelPortal; P9WIE5; -.
SMR; P9WIE5; -.
STRING; 83332.Rv1908c; -.
PaxDb; P9WIE5; -.
EnsemblBacteria; CCP44675; CCP44675; Rv1908c.
GeneID; 885638; -.
KEGG; mtu:Rv1908c; -.
TubercuList; Rv1908c; -.
eggNOG; ENOG4105C1X; Bacteria.
eggNOG; COG0376; LUCA.
KO; K03782; -.
OMA; PEEDIYW; -.
PhylomeDB; P9WIE5; -.
BioCyc; MetaCyc:G185E-6105-MONOMER; -.
Reactome; R-HSA-1222387; Tolerance of reactive oxygen produced by macrophages.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0004096; F:catalase activity; IDA:MTBBASE.
GO; GO:0020037; F:heme binding; IDA:MTBBASE.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070404; F:NADH binding; IDA:MTBBASE.
GO; GO:0070402; F:NADPH binding; IDA:MTBBASE.
GO; GO:0016677; F:oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor; IDA:MTBBASE.
GO; GO:0004601; F:peroxidase activity; IDA:MTBBASE.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0052059; P:evasion or tolerance by symbiont of host-produced reactive oxygen species; TAS:Reactome.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0045739; P:positive regulation of DNA repair; IGI:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IMP:MTBBASE.
HAMAP; MF_01961; Catal_peroxid; 1.
InterPro; IPR000763; Catalase_peroxidase.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
PANTHER; PTHR30555; PTHR30555; 1.
Pfam; PF00141; peroxidase; 2.
PRINTS; PR00460; BPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 2.
TIGRFAMs; TIGR00198; cat_per_HPI; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome; Heme;
Hydrogen peroxide; Iron; Metal-binding; Organic radical;
Oxidoreductase; Peroxidase; Reference proteome; Virulence.
CHAIN 1 740 Catalase-peroxidase.
/FTId=PRO_0000055574.
ACT_SITE 108 108 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01961}.
ACT_SITE 321 321 Tryptophan radical intermediate.
{ECO:0000269|PubMed:18052167}.
METAL 270 270 Iron (heme axial ligand); via tele
nitrogen. {ECO:0000244|PDB:1SJ2,
ECO:0000244|PDB:2CCA,
ECO:0000244|PDB:2CCD,
ECO:0000244|PDB:4C51,
ECO:0000269|PubMed:15231843,
ECO:0000269|PubMed:16566587,
ECO:0000269|PubMed:24185282}.
SITE 104 104 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01961}.
CROSSLNK 107 229 Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
(with M-255); alternate.
{ECO:0000255|HAMAP-Rule:MF_01961,
ECO:0000269|PubMed:15231843}.
CROSSLNK 229 255 Tryptophyl-tyrosyl-methioninium (Tyr-Met)
(with W-107); alternate.
{ECO:0000255|HAMAP-Rule:MF_01961,
ECO:0000269|PubMed:15231843}.
VARIANT 300 300 W -> G (in strain: H0892/92; INH-
resistant).
VARIANT 315 315 S -> T (in strain: H0181/94, H0452/92,
H0948/92 and H0169/93; INH-resistant).
VARIANT 463 463 R -> L (in strain: H0169/93; INH-
resistant).
VARIANT 501 501 P -> A (in strain: H0948/92; INH-
resistant).
VARIANT 525 525 Q -> P (in strain: H0251/90; INH-
resistant).
VARIANT 587 587 L -> P (in strain: 15726/89; INH-
resistant).
VARIANT 700 700 S -> P (in strain: H0004/93; INH-
resistant).
MUTAGEN 137 137 D->S: Exhibits 8-fold increased catalytic
efficiency for the activation of INH
(INH-NAD formation). Possesses an
enlarged substrate access channel.
{ECO:0000269|PubMed:24185282}.
MUTAGEN 229 229 Y->F: Exhibits 2-fold increased affinity
for INH. {ECO:0000269|PubMed:24185282}.
MUTAGEN 315 315 S->T: 20-fold decrease in the rate of
INH-NAD adduct formation. Exhibits
significantly reduced affinity for INH
(KM is increased by 43-fold).
{ECO:0000269|PubMed:16566587,
ECO:0000269|PubMed:24185282}.
MUTAGEN 321 321 W->F: Nearly no effect on the kinetic
parameters for the activation of INH.
{ECO:0000269|PubMed:24185282}.
MUTAGEN 418 418 R->L: Exhibits 1.7-fold decreased
catalytic efficiency for the activation
of INH. {ECO:0000269|PubMed:24185282}.
MUTAGEN 463 463 R->L: Nearly no effect on the kinetic
parameters for the catalase and
peroxidase activity. Activates INH and
mediates InhA inactivation as efficiently
as wild-type.
{ECO:0000269|PubMed:9006925}.
CONFLICT 234 234 G -> A (in Ref. 1; CAA48213).
{ECO:0000305}.
CONFLICT 500 512 QPQVGWEVNDPDG -> CSHKSGGRSTTRR (in Ref.
9; AAA72374). {ECO:0000305}.
HELIX 29 31 {ECO:0000244|PDB:2CCA}.
HELIX 35 37 {ECO:0000244|PDB:2CCA}.
HELIX 45 48 {ECO:0000244|PDB:2CCA}.
HELIX 53 55 {ECO:0000244|PDB:2CCA}.
HELIX 64 68 {ECO:0000244|PDB:2CCA}.
HELIX 73 84 {ECO:0000244|PDB:2CCA}.
HELIX 94 96 {ECO:0000244|PDB:2CCA}.
HELIX 99 110 {ECO:0000244|PDB:2CCA}.
TURN 115 117 {ECO:0000244|PDB:2CCA}.
HELIX 122 124 {ECO:0000244|PDB:2CCD}.
HELIX 126 128 {ECO:0000244|PDB:2CCA}.
HELIX 132 134 {ECO:0000244|PDB:2CCA}.
HELIX 136 138 {ECO:0000244|PDB:2CCA}.
HELIX 141 146 {ECO:0000244|PDB:2CCA}.
HELIX 149 155 {ECO:0000244|PDB:2CCA}.
HELIX 156 158 {ECO:0000244|PDB:2CCA}.
HELIX 161 175 {ECO:0000244|PDB:2CCA}.
TURN 212 214 {ECO:0000244|PDB:2CCA}.
STRAND 222 224 {ECO:0000244|PDB:2CCA}.
STRAND 228 230 {ECO:0000244|PDB:2CCA}.
HELIX 235 237 {ECO:0000244|PDB:2CCA}.
HELIX 241 253 {ECO:0000244|PDB:2CCA}.
TURN 254 256 {ECO:0000244|PDB:2CCA}.
HELIX 259 270 {ECO:0000244|PDB:2CCA}.
STRAND 277 279 {ECO:0000244|PDB:2CCA}.
HELIX 281 283 {ECO:0000244|PDB:2CCA}.
HELIX 288 290 {ECO:0000244|PDB:2CCA}.
HELIX 293 295 {ECO:0000244|PDB:2CCA}.
HELIX 309 311 {ECO:0000244|PDB:2CCA}.
STRAND 313 316 {ECO:0000244|PDB:2CCA}.
HELIX 331 338 {ECO:0000244|PDB:2CCA}.
STRAND 341 345 {ECO:0000244|PDB:2CCA}.
STRAND 351 355 {ECO:0000244|PDB:2CCA}.
HELIX 356 358 {ECO:0000244|PDB:2CCA}.
TURN 359 362 {ECO:0000244|PDB:2CCA}.
STRAND 367 369 {ECO:0000244|PDB:1SJ2}.
HELIX 379 386 {ECO:0000244|PDB:2CCA}.
HELIX 388 399 {ECO:0000244|PDB:2CCA}.
HELIX 401 417 {ECO:0000244|PDB:2CCA}.
HELIX 418 420 {ECO:0000244|PDB:1SJ2}.
HELIX 423 425 {ECO:0000244|PDB:2CCA}.
HELIX 437 439 {ECO:0000244|PDB:2CCA}.
HELIX 452 463 {ECO:0000244|PDB:2CCA}.
TURN 464 466 {ECO:0000244|PDB:2CCA}.
HELIX 469 480 {ECO:0000244|PDB:2CCA}.
TURN 485 488 {ECO:0000244|PDB:2CCA}.
HELIX 496 498 {ECO:0000244|PDB:2CCA}.
HELIX 502 504 {ECO:0000244|PDB:2CCA}.
TURN 510 513 {ECO:0000244|PDB:2CCA}.
HELIX 514 531 {ECO:0000244|PDB:2CCA}.
STRAND 533 536 {ECO:0000244|PDB:1SJ2}.
HELIX 540 558 {ECO:0000244|PDB:2CCA}.
HELIX 576 578 {ECO:0000244|PDB:2CCA}.
HELIX 581 584 {ECO:0000244|PDB:2CCA}.
HELIX 585 587 {ECO:0000244|PDB:2CCA}.
STRAND 590 592 {ECO:0000244|PDB:2CCA}.
HELIX 593 595 {ECO:0000244|PDB:2CCA}.
HELIX 606 616 {ECO:0000244|PDB:2CCA}.
HELIX 621 633 {ECO:0000244|PDB:2CCA}.
HELIX 638 640 {ECO:0000244|PDB:2CCA}.
HELIX 656 661 {ECO:0000244|PDB:2CCA}.
STRAND 667 670 {ECO:0000244|PDB:2CCA}.
STRAND 675 681 {ECO:0000244|PDB:2CCA}.
STRAND 683 685 {ECO:0000244|PDB:2CCD}.
STRAND 687 692 {ECO:0000244|PDB:2CCA}.
HELIX 693 700 {ECO:0000244|PDB:2CCA}.
HELIX 702 711 {ECO:0000244|PDB:2CCA}.
HELIX 717 732 {ECO:0000244|PDB:2CCA}.
TURN 733 735 {ECO:0000244|PDB:2CCA}.
HELIX 737 739 {ECO:0000244|PDB:2CCA}.
SEQUENCE 740 AA; 80605 MW; B43C033B533CDD89 CRC64;
MPEQHPPITE TTTGAASNGC PVVGHMKYPV EGGGNQDWWP NRLNLKVLHQ NPAVADPMGA
AFDYAAEVAT IDVDALTRDI EEVMTTSQPW WPADYGHYGP LFIRMAWHAA GTYRIHDGRG
GAGGGMQRFA PLNSWPDNAS LDKARRLLWP VKKKYGKKLS WADLIVFAGN CALESMGFKT
FGFGFGRVDQ WEPDEVYWGK EATWLGDERY SGKRDLENPL AAVQMGLIYV NPEGPNGNPD
PMAAAVDIRE TFRRMAMNDV ETAALIVGGH TFGKTHGAGP ADLVGPEPEA APLEQMGLGW
KSSYGTGTGK DAITSGIEVV WTNTPTKWDN SFLEILYGYE WELTKSPAGA WQYTAKDGAG
AGTIPDPFGG PGRSPTMLAT DLSLRVDPIY ERITRRWLEH PEELADEFAK AWYKLIHRDM
GPVARYLGPL VPKQTLLWQD PVPAVSHDLV GEAEIASLKS QIRASGLTVS QLVSTAWAAA
SSFRGSDKRG GANGGRIRLQ PQVGWEVNDP DGDLRKVIRT LEEIQESFNS AAPGNIKVSF
ADLVVLGGCA AIEKAAKAAG HNITVPFTPG RTDASQEQTD VESFAVLEPK ADGFRNYLGK
GNPLPAEYML LDKANLLTLS APEMTVLVGG LRVLGANYKR LPLGVFTEAS ESLTNDFFVN
LLDMGITWEP SPADDGTYQG KDGSGKVKWT GSRVDLVFGS NSELRALVEV YGADDAQPKF
VQDFVAAWDK VMNLDRFDVR


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