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Protein

Catalase-peroxidase

Gene

katG

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May 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.UniRule annotation1 Publication

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Kineticsi

  1. KM=225 mM for H2O2 for the catalase reaction (at pH 5.5-6.0)1 Publication
  2. KM=2.4 mM for H2O2 for the catalase reaction (at pH 7.0)1 Publication
  3. KM=360 µM for H2O2 for the peroxidase reaction1 Publication
  4. KM=67 µM for ABTS for the peroxidase reaction1 Publication
  1. Vmax=7620 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0)1 Publication
  2. Vmax=5700 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0)1 Publication
  3. Vmax=14 µmol/min/mg enzyme for ABTS for the peroxidase reaction1 Publication

pH dependencei

Optimum pH is 4.75 for the peroxidase reaction.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei104 – 1041Transition state stabilizer
Active sitei108 – 1081Proton acceptor
Metal bindingi270 – 2701Iron (heme axial ligand)
Active sitei321 – 3211Tryptophan radical intermediate

GO - Molecular functioni

  • catalase activity Source: MTBBASE
  • heme binding Source: MTBBASE
  • metal ion binding Source: UniProtKB-KW
  • NADH binding Source: MTBBASE
  • NADPH binding Source: MTBBASE
  • oxidoreductase activity, acting on a heme group of donors, nitrogenous group as acceptor Source: MTBBASE
  • peroxidase activity Source: MTBBASE

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • cellular response to hydrogen peroxide Source: GO_Central
  • evasion or tolerance by symbiont of host-produced reactive oxygen species Source: Reactome
  • hydrogen peroxide catabolic process Source: MTBBASE
  • response to antibiotic Source: UniProtKB-KW
  • response to oxidative stress Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Antibiotic resistance, Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1222387. Tolerance of reactive oxygen produced by macrophages.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:Rv1908c
ORF Names:MTCY180.10
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1908c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells show isoniazid (INH) resistance and are more sensitive to oxidative stress.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Catalase-peroxidasePRO_0000055574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki107 ↔ 229Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255); alternate
Cross-linki229 ↔ 255Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107); alternate

Post-translational modificationi

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

Keywords - PTMi

Organic radical

Proteomic databases

PaxDbiP9WIE5.

Expressioni

Inductioni

By treatment with H2O2. Repressed by FurA.2 Publications

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv1908c.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Helixi35 – 373Combined sources
Helixi45 – 484Combined sources
Helixi53 – 553Combined sources
Helixi64 – 685Combined sources
Helixi73 – 8412Combined sources
Helixi94 – 963Combined sources
Helixi99 – 11012Combined sources
Turni115 – 1173Combined sources
Helixi122 – 1243Combined sources
Helixi126 – 1283Combined sources
Helixi132 – 1343Combined sources
Helixi136 – 1383Combined sources
Helixi141 – 1466Combined sources
Helixi149 – 1557Combined sources
Helixi156 – 1583Combined sources
Helixi161 – 17515Combined sources
Turni212 – 2143Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi228 – 2303Combined sources
Helixi235 – 2373Combined sources
Helixi241 – 25313Combined sources
Turni254 – 2563Combined sources
Helixi259 – 27012Combined sources
Beta strandi277 – 2793Combined sources
Helixi281 – 2833Combined sources
Helixi288 – 2903Combined sources
Helixi293 – 2953Combined sources
Helixi309 – 3113Combined sources
Beta strandi313 – 3164Combined sources
Helixi331 – 3388Combined sources
Beta strandi341 – 3455Combined sources
Beta strandi351 – 3555Combined sources
Helixi356 – 3583Combined sources
Turni359 – 3624Combined sources
Beta strandi367 – 3693Combined sources
Helixi379 – 3868Combined sources
Helixi388 – 39912Combined sources
Helixi401 – 41717Combined sources
Helixi418 – 4203Combined sources
Helixi423 – 4253Combined sources
Helixi437 – 4393Combined sources
Helixi452 – 46312Combined sources
Turni464 – 4663Combined sources
Helixi469 – 48012Combined sources
Turni485 – 4884Combined sources
Helixi496 – 4983Combined sources
Helixi502 – 5043Combined sources
Turni510 – 5134Combined sources
Helixi514 – 53118Combined sources
Beta strandi533 – 5364Combined sources
Helixi540 – 55819Combined sources
Helixi576 – 5783Combined sources
Helixi581 – 5844Combined sources
Helixi585 – 5873Combined sources
Beta strandi590 – 5923Combined sources
Helixi593 – 5953Combined sources
Helixi606 – 61611Combined sources
Helixi621 – 63313Combined sources
Helixi638 – 6403Combined sources
Helixi656 – 6616Combined sources
Beta strandi667 – 6704Combined sources
Beta strandi675 – 6817Combined sources
Beta strandi683 – 6853Combined sources
Beta strandi687 – 6926Combined sources
Helixi693 – 7008Combined sources
Helixi702 – 71110Combined sources
Helixi717 – 73216Combined sources
Turni733 – 7353Combined sources
Helixi737 – 7393Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SFZmodel-A1-740[»]
1SJ2X-ray2.41A/B2-740[»]
2CCAX-ray2.00A/B1-740[»]
2CCDX-ray2.10A/B1-740[»]
4C50X-ray2.50A/B1-740[»]
4C51X-ray3.10A/B1-740[»]
ProteinModelPortaliP9WIE5.
SMRiP9WIE5. Positions 26-740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
KOiK03782.
OMAiTESKCPF.
PhylomeDBiP9WIE5.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P9WIE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEQHPPITE TTTGAASNGC PVVGHMKYPV EGGGNQDWWP NRLNLKVLHQ
60 70 80 90 100
NPAVADPMGA AFDYAAEVAT IDVDALTRDI EEVMTTSQPW WPADYGHYGP
110 120 130 140 150
LFIRMAWHAA GTYRIHDGRG GAGGGMQRFA PLNSWPDNAS LDKARRLLWP
160 170 180 190 200
VKKKYGKKLS WADLIVFAGN CALESMGFKT FGFGFGRVDQ WEPDEVYWGK
210 220 230 240 250
EATWLGDERY SGKRDLENPL AAVQMGLIYV NPEGPNGNPD PMAAAVDIRE
260 270 280 290 300
TFRRMAMNDV ETAALIVGGH TFGKTHGAGP ADLVGPEPEA APLEQMGLGW
310 320 330 340 350
KSSYGTGTGK DAITSGIEVV WTNTPTKWDN SFLEILYGYE WELTKSPAGA
360 370 380 390 400
WQYTAKDGAG AGTIPDPFGG PGRSPTMLAT DLSLRVDPIY ERITRRWLEH
410 420 430 440 450
PEELADEFAK AWYKLIHRDM GPVARYLGPL VPKQTLLWQD PVPAVSHDLV
460 470 480 490 500
GEAEIASLKS QIRASGLTVS QLVSTAWAAA SSFRGSDKRG GANGGRIRLQ
510 520 530 540 550
PQVGWEVNDP DGDLRKVIRT LEEIQESFNS AAPGNIKVSF ADLVVLGGCA
560 570 580 590 600
AIEKAAKAAG HNITVPFTPG RTDASQEQTD VESFAVLEPK ADGFRNYLGK
610 620 630 640 650
GNPLPAEYML LDKANLLTLS APEMTVLVGG LRVLGANYKR LPLGVFTEAS
660 670 680 690 700
ESLTNDFFVN LLDMGITWEP SPADDGTYQG KDGSGKVKWT GSRVDLVFGS
710 720 730 740
NSELRALVEV YGADDAQPKF VQDFVAAWDK VMNLDRFDVR
Length:740
Mass (Da):80,605
Last modified:April 16, 2014 - v1
Checksum:iB43C033B533CDD89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341G → A in CAA48213 (PubMed:8320241).Curated
Sequence conflicti500 – 51213QPQVG…NDPDG → CSHKSGGRSTTRR in AAA72374 (PubMed:10463167).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti300 – 3001W → G in strain: H0892/92; INH-resistant.
Natural varianti315 – 3151S → T in strain: H0181/94, H0452/92, H0948/92 and H0169/93; INH-resistant.
Natural varianti463 – 4631R → L in strain: H0169/93; INH-resistant.
Natural varianti501 – 5011P → A in strain: H0948/92; INH-resistant.
Natural varianti525 – 5251Q → P in strain: H0251/90; INH-resistant.
Natural varianti587 – 5871L → P in strain: 15726/89; INH-resistant.
Natural varianti700 – 7001S → P in strain: H0004/93; INH-resistant.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68081 Genomic DNA. Translation: CAA48213.1.
U06258 Unassigned DNA. Translation: AAB04159.1.
U40593 Genomic DNA. Translation: AAA85167.1.
U40595 Genomic DNA. Translation: AAA85169.1.
U41305 Genomic DNA. Translation: AAA85171.1.
U41306 Genomic DNA. Translation: AAA85172.1.
U41307 Genomic DNA. Translation: AAA85173.1.
U41308 Genomic DNA. Translation: AAA85174.1.
U41309 Genomic DNA. Translation: AAA85175.1.
U41310 Genomic DNA. Translation: AAA85176.1.
U41311 Genomic DNA. Translation: AAA85177.1.
U41312 Genomic DNA. Translation: AAA85178.1.
U41313 Genomic DNA. Translation: AAA85179.1.
U41314 Genomic DNA. Translation: AAA85180.1.
JX303265 Genomic DNA. Translation: AFR90354.1.
JX303270 Genomic DNA. Translation: AFR90359.1.
JX303273 Genomic DNA. Translation: AFR90362.1.
JX303276 Genomic DNA. Translation: AFR90365.1.
JX303277 Genomic DNA. Translation: AFR90366.1.
JX303278 Genomic DNA. Translation: AFR90367.1.
JX303280 Genomic DNA. Translation: AFR90369.1.
AL123456 Genomic DNA. Translation: CCP44675.1.
AF002194 Genomic DNA. Translation: AAB63371.1.
L14268 Genomic DNA. Translation: AAA72374.1.
PIRiA70519. A40662.
RefSeqiNP_216424.1. NC_000962.3.
WP_003899075.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44675; CCP44675; Rv1908c.
GeneIDi885638.
KEGGimtu:Rv1908c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68081 Genomic DNA. Translation: CAA48213.1.
U06258 Unassigned DNA. Translation: AAB04159.1.
U40593 Genomic DNA. Translation: AAA85167.1.
U40595 Genomic DNA. Translation: AAA85169.1.
U41305 Genomic DNA. Translation: AAA85171.1.
U41306 Genomic DNA. Translation: AAA85172.1.
U41307 Genomic DNA. Translation: AAA85173.1.
U41308 Genomic DNA. Translation: AAA85174.1.
U41309 Genomic DNA. Translation: AAA85175.1.
U41310 Genomic DNA. Translation: AAA85176.1.
U41311 Genomic DNA. Translation: AAA85177.1.
U41312 Genomic DNA. Translation: AAA85178.1.
U41313 Genomic DNA. Translation: AAA85179.1.
U41314 Genomic DNA. Translation: AAA85180.1.
JX303265 Genomic DNA. Translation: AFR90354.1.
JX303270 Genomic DNA. Translation: AFR90359.1.
JX303273 Genomic DNA. Translation: AFR90362.1.
JX303276 Genomic DNA. Translation: AFR90365.1.
JX303277 Genomic DNA. Translation: AFR90366.1.
JX303278 Genomic DNA. Translation: AFR90367.1.
JX303280 Genomic DNA. Translation: AFR90369.1.
AL123456 Genomic DNA. Translation: CCP44675.1.
AF002194 Genomic DNA. Translation: AAB63371.1.
L14268 Genomic DNA. Translation: AAA72374.1.
PIRiA70519. A40662.
RefSeqiNP_216424.1. NC_000962.3.
WP_003899075.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SFZmodel-A1-740[»]
1SJ2X-ray2.41A/B2-740[»]
2CCAX-ray2.00A/B1-740[»]
2CCDX-ray2.10A/B1-740[»]
4C50X-ray2.50A/B1-740[»]
4C51X-ray3.10A/B1-740[»]
ProteinModelPortaliP9WIE5.
SMRiP9WIE5. Positions 26-740.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1908c.

Proteomic databases

PaxDbiP9WIE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44675; CCP44675; Rv1908c.
GeneIDi885638.
KEGGimtu:Rv1908c.

Organism-specific databases

TubercuListiRv1908c.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
KOiK03782.
OMAiTESKCPF.
PhylomeDBiP9WIE5.

Enzyme and pathway databases

ReactomeiR-HSA-1222387. Tolerance of reactive oxygen produced by macrophages.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis."
    Heym B., Zhang Y., Poulet S., Young D., Cole S.T.
    J. Bacteriol. 175:4255-4259(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 25618 / H37Rv.
  2. Cole S.T.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Rapid identification of a point mutation of the Mycobacterium tuberculosis catalase-peroxidase (katG) gene associated with isoniazid resistance."
    Cockerill F.R. III, Uhl J.R., Temesgen Z., Zhang Y., Stockman L., Roberts G.D., Williams D.L., Kline B.C.
    J. Infect. Dis. 171:240-245(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  4. "katG gene mutations in isoniazid-resistant Mycobacterium tuberculosis strains isolated from Finnish patients."
    Marttila H.J., Soini H., Huovinen P., Viljanen M.K.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: INH-resistant strains.
  5. "Next-generation ion torrent sequencing of drug resistance mutations in Mycobacterium tuberculosis strains."
    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.
    J. Clin. Microbiol. 50:3831-3837(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 2937643, 3150565, 3264812, MTB001, MTB003, MTB005 and MTB007.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  7. "The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis."
    Zhang Y., Heym B., Allen B., Young D., Cole S.T.
    Nature 358:591-593(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ISONIAZID RESISTANCE, DISRUPTION PHENOTYPE.
    Strain: ATCC 25618 / H37Rv.
  8. Song J., Deretic V.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
    Strain: ATCC 25618 / H37Rv.
  9. "Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents."
    Mulder M.A., Nair S., Abratt V.R., Zappe H., Steyn L.M.
    Microbiology 145:2011-2021(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-740, FUNCTION.
    Strain: ATCC 25618 / H37Rv.
  10. "Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis."
    Sherman D.R., Mdluli K., Hickey M.J., Arain T.M., Morris S.L., Barry C.E. III, Stover C.K.
    Science 272:1641-1643(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis."
    Pym A.S., Domenech P., Honore N., Song J., Deretic V., Cole S.T.
    Mol. Microbiol. 40:879-889(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC 25618 / H37Rv.
  12. "The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties."
    Ghiladi R.A., Knudsen G.M., Medzihradszky K.F., Ortiz de Montellano P.R.
    J. Biol. Chem. 280:22651-22663(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT BOND.
  13. "Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis."
    Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C.
    Biochemistry 46:1183-1193(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC MECHANISM.
  14. "Two [Fe(IV)=O Trp*] intermediates in M.tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: reactivity toward isoniazid."
    Singh R., Switala J., Loewen P.C., Ivancich A.
    J. Am. Chem. Soc. 129:15954-15963(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: RADICAL INTERMEDIATE.
  15. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  16. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 2-740.
  19. "Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant."
    Zhao X., Yu H., Yu S., Wang F., Sacchettini J.C., Magliozzo R.S.
    Biochemistry 45:4131-4140(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF WILD-TYPE AND OF VARIANT THR-315 IN COMPLEX WITH HEME.

Entry informationi

Entry nameiKATG_MYCTU
AccessioniPrimary (citable) accession number: P9WIE5
Secondary accession number(s): J9VFD2
, O08221, Q08129, Q50544, Q50546, Q50551, Q50552, Q50553, Q50554, Q50555, Q50762, Q57215, Q57274
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to the Synechocystis sp. enzyme, no Trp radical is formed on the distal Trp residue (Trp-91).
The action of antitubercular drug isoniazid (INH) is dependent on its activation by KatG to form an isonicotinoyl-NAD adduct (IN-NAD). Resistance to INH can be due to mutations that reduces KatG activity.
Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.