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Reviewed, UniProtKB/Swiss-Prot P46817 (KATG_MYCBO)

Last modified November 25, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase
Gene names
Name: katG
Ordered Locus Names: Mb1943c
OrganismMycobacterium bovis [Complete proteome] [HAMAP]
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length740 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria.

Catalytic activity

2 H(2)O(2) = O(2) + 2 H(2)O.

Donor + H(2)O(2) = oxidized donor + 2 H(2)O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity.

Subunit structure

Homodimer.

Post-translational modification

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

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords

   Biological processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 740740Catalase-peroxidase
PRO_0000055571

Sites

Active site1081Proton acceptor By similarity
Metal binding2701Iron (heme axial ligand) By similarity
Site1041Transition state stabilizer By similarity

Amino acid modifications

Cross-link107 ↔ 229Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) By similarity
Cross-link229 ↔ 255Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) By similarity

Experimental info

Sequence conflict2341G → A in CAA58266. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46817-1 [UniParc].

Last modified July 11, 2003. Version 2.
Checksum: 8231F1E473397908

FASTA74080,562
        10         20         30         40         50         60 
MPEQHPPITE TTTGAASNGC PVVGHMKYPV EGGGNQDWWP NRLNLKVLHQ NPAVADPMGA 

        70         80         90        100        110        120 
AFDYAAEVAT IDVDALTRDI EEVMTTSQPW WPADYGHYGP LFIRMAWHAA GTYRIHDGRG 

       130        140        150        160        170        180 
GAGGGMQRFA PLNSWPDNAS LDKARRLLWP VKKKYGKKLS WADLIVFAGN CALESMGFKT 

       190        200        210        220        230        240 
FGFGFGRVDQ WEPDEVYWGK EATWLGDERY SGKRDLENPL AAVQMGLIYV NPEGPNGNPD 

       250        260        270        280        290        300 
PMAAAVDIRE TFRRMAMNDV ETAALIVGGH TFGKTHGAGP ADLVGPEPEA APLEQMGLGW 

       310        320        330        340        350        360 
KSSYGTGTGK DAITSGIEVV WTNTPTKWDN SFLEILYGYE WELTKSPAGA WQYTAKDGAG 

       370        380        390        400        410        420 
AGTIPDPFGG PGRSPTMLAT DLSLRVDPIY ERITRRWLEH PEELADEFAK AWYKLIHRDM 

       430        440        450        460        470        480 
GPVARYLGPL VPKQTLLWQD PVPAVSHDLV GEAEIASLKS QILASGLTVS QLVSTAWAAA 

       490        500        510        520        530        540 
SSFRGSDKRG GANGGRIRLQ PQVGWEVNDP DGDLRKVIRT LEEIQESFNS AAPGNIKVSF 

       550        560        570        580        590        600 
ADLVVLGGCA AIEKAAKAAG HNITVPFTPG RTDASQEQTD VESFAVLEPK ADGFRNYLGK 

       610        620        630        640        650        660 
GNPLPAEYML LDKANLLTLS APEMTVLVGG LRVLGANYKR LPLGVFTEAS ESLTNDFFVN 

       670        680        690        700        710        720 
LLDMGITWEP SPADDGTYQG KDGSGKVKWT GSRVDLVFGS NSELRALVEV YGADDAQPKF 

       730        740 
VQDFVAAWDK VMNLDRFDVR 

« Hide

References

« Hide 'large scale' references
[1]"Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis."
Heym B., Alzari P.M., Honore N., Cole S.T.
Mol. Microbiol. 15:235-245(1995) [PubMed: 7746145] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BCG.
[2]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.
[3]"Catalase-peroxidase of Mycobacterium bovis BCG converts isoniazid to isonicotinamide, but not to isonicotinic acid: differentiation parameter between enzymes of Mycobacterium bovis BCG and Mycobacterium tuberculosis."
Kang S.-K., Lee J.-H., Lee Y.-C., Kim C.-H.
Biochim. Biophys. Acta 1760:724-729(2006) [PubMed: 16563633] [Abstract]
Cited for: FUNCTION, SUBUNIT.

Cross-references

Sequence databases

X83277 Genomic DNA. Translation: CAA58266.1.
BX248340 Genomic DNA. Translation: CAD94645.1.
RefSeqNP_855594.1.

3D structure databases

HSSPHSSP built from PDB template 1MWV based on UniProtKB Q939D2.
SMRP46817. Positions 26-740.
ModBaseSearch...

Protein family/group databases

PeroxiBase2434. MboCP01_BCG.
4578. MboCP01_AF2122.

Genome annotation databases

GeneID1093267.
GenomeReviewsGene locus Mb1943c in contig BX248333_GR.
KEGGmbo:Mb1943c.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP46817.

Family and domain databases

HAMAPMF_01961.
[Tree]
InterProIPR000763. Catalase_proxase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
TIGRFAMsTIGR00198. cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_MYCBO
AccessionPrimary (citable) accession number: P46817
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2003
Last modified: November 25, 2008
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents