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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
 
 
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