KATG_MYCTE
ID KATG_MYCTE Reviewed; 740 AA.
AC H8F3Q9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 46.
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};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=ERDMAN_2101;
OS Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=652616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=22535945; DOI=10.1128/jb.00353-12;
RA Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL J. Bacteriol. 194:2770-2770(2012).
RN [2]
RP FUNCTION IN PATHOGENESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=15165233; DOI=10.1111/j.1365-2958.2004.04078.x;
RA Ng V.H., Cox J.S., Sousa A.O., MacMicking J.D., McKinney J.D.;
RT "Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering
RT the phagocyte oxidative burst.";
RL Mol. Microbiol. 52:1291-1302(2004).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT three anti-sigma factor substrates.";
RL Mol. Microbiol. 77:605-617(2010).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity, oxidizing various electron donors including
CC NADP(H) (By similarity). Protects M.tuberculosis against toxic reactive
CC oxygen species (ROS) including hydrogen peroxide as well as organic
CC peroxides and thus contributes to its survival within host macrophages
CC by countering the phagocyte oxidative burst (PubMed:15165233). Also
CC displays efficient peroxynitritase activity, which may help the
CC bacterium to persist in macrophages (By similarity).
CC {ECO:0000250|UniProtKB:P9WIE5, ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:15165233}.
CC -!- FUNCTION: Catalyzes the oxidative activation of the antitubercular pro-
CC drug isoniazid (INH) to generate an isonicotinoyl radical that then
CC reacts nonenzymatically with NAD to form an isonicotinoyl-NAD adduct
CC which inhibits InhA. {ECO:0000250|UniProtKB:P9WIE5}.
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 -!- 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 -!- 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. {ECO:0000250|UniProtKB:P9WIE5}.
CC -!- INDUCTION: By the metal chelator phenanthroline via Rip1, RskA/SigK and
CC RslA/SigL. {ECO:0000269|PubMed:20545848}.
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 lacking this gene are devoid of catalase
CC activity, supersensitive to H(2)O(2) exposure and highly resistant to
CC the antitubercular drug isoniazid (INH) in vitro. This mutant strain is
CC markedly attenuated for virulence in mice and displays impaired growth
CC in infected macrophages, but its growth and survival is
CC indistinguishable from wild-type in macrophages lacking the ROS-
CC generating NADPH oxidase (Phox). {ECO:0000269|PubMed:15165233}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; AP012340; BAL65894.1; -; Genomic_DNA.
DR RefSeq; WP_003899075.1; NZ_KK339487.1.
DR AlphaFoldDB; H8F3Q9; -.
DR SMR; H8F3Q9; -.
DR EnsemblBacteria; BAL65894; BAL65894; ERDMAN_2101.
DR KEGG; mtn:ERDMAN_2101; -.
DR PATRIC; fig|652616.3.peg.2136; -.
DR HOGENOM; CLU_025424_2_0_11; -.
DR Proteomes; UP000007568; 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 1: Evidence at protein level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Organic radical;
KW Oxidoreductase; Peroxidase; Virulence.
FT CHAIN 1..740
FT /note="Catalase-peroxidase"
FT /id="PRO_0000422688"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT ACT_SITE 321
FT /note="Tryptophan radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WIE5"
FT BINDING 270
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 104
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 107..229
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 255)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 229..255
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 107)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ 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
