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Reviewed, UniProtKB/Swiss-Prot A0QXX7 (KATG2_MYCS2)

Last modified November 3, 2009. Version 26. 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 2
      Short name=CP 2
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 2
Gene names
Name: katG2
Synonyms: katH
Ordered Locus Names: MSMEG_3461
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Complete proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. HAMAP MF_01961

Catalytic activity

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961

Cofactor

Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer. Ref.3

Subunit structure

Homotetramer. Ref.3

Post-translational modification

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

Disruption phenotype

Defects cause isoniazid (INH) resistance. Ref.3

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=1.4 mM for H2O2 for the catalase reaction HAMAP MF_01961

KM=0.19 mM for o-dianisidine for the peroxidase reaction

KM=0.17 mM for NADPH for the peroxidase reaction

KM=0.23 mM for NADH for the peroxidase reaction

KM=0.31 mM for pyrogallol for the peroxidase reaction

KM=0.11 mM for 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) for the peroxidase reaction

Mass spectrometry

Molecular mass is 81889 Da from positions 2 - 748. Determined by ESI. Ref.3

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 748747Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000345094

Sites

Active site1141Proton acceptor By similarity
Metal binding2791Iron (heme axial ligand) By similarity
Site1101Transition state stabilizer By similarity

Amino acid modifications

Cross-link113 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) By similarity
Cross-link238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-113) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QXX7-1 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 73E44205C96B2FD3

FASTA74881,998
        10         20         30         40         50         60 
MSSDTSDSRP PNPDTKTAST SESENPAIPS PKPKSGAPLR NQDWWPNQID VSRLHPHPPQ 

        70         80         90        100        110        120 
GNPLGEDFDY AEEFAKLDVN ALKADLTALM TQSQDWWPAD YGHYGGLFIR MSWHSAGTYR 

       130        140        150        160        170        180 
IHDGRGGGGQ GAQRFAPINS WPDNVSLDKA RRLLWPIKQK YGNKISWADL LVFTGNVALE 

       190        200        210        220        230        240 
SMGFKTFGFG FGREDIWEPE EILFGEEDEW LGTDKRYGGG EQRQLAEPYG ATTMGLIYVN 

       250        260        270        280        290        300 
PEGPEGQPDP LAAAHDIRET FGRMAMNDEE TAALIVGGHT FGKTHGAGDA SLVGPEPEAA 

       310        320        330        340        350        360 
PIEQQGLGWK SSYGTGKGPD TITSGLEVVW TNTPTKWDNS FLEILYGYEW ELTKSPAGAW 

       370        380        390        400        410        420 
QFTAKDGAGA GTIPDPFGGP GRNPTMLVTD ISMRVDPIYG KITRRWLDHP EELSEAFAKA 

       430        440        450        460        470        480 
WYKLLHRDMG PISRYLGPWV AEPQLWQDPV PAVDHPLVDD QDIAALKSTV LDSGLSTGQL 

       490        500        510        520        530        540 
IKTAWASAAS YRNTDKRGGA NGARVRLEPQ KNWDVNEPAE LATVLPVLER IQQDFNASAS 

       550        560        570        580        590        600 
GGKKVSLADL IVLAGSAAIE KAAKDGGYNV TVPFAPGRTD ASQENTDVES FAVLEPRADG 

       610        620        630        640        650        660 
FRNYVRPGEK VQLEKMLLER AYFLGVTAPQ LTALVGGLRA LDVNHGGTKH GVFTDRPGAL 

       670        680        690        700        710        720 
TNDFFVNLLD MGTEWKTSET TENVYEGVDR KTGQLKWTAT ANDLVFGSHS VLRAVAEVYA 

       730        740 
QSDNGERFVN DFVKAWVKVM NNDRFDLK 

« Hide

References

« Hide 'large scale' references
[1]"The catalase-peroxidase of Mycobacterium smegmatis."
Honore N.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation."
Marcinkeviciene J.A., Magliozzo R.S., Blanchard J.S.
J. Biol. Chem. 270:22290-22295(1995) [PubMed: 7673210] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20, BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT, MASS SPECTROMETRY, DISRUPTION PHENOTYPE.
[4]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed: 18955433] [Abstract]
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS] BY MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.

Cross-references

Sequence databases

AJ311851 Genomic DNA. Translation: CAC44462.1.
CP000480 Genomic DNA. Translation: ABK73887.1.
RefSeqYP_887765.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0QXX7.

Genome annotation databases

GeneID4536428.
GenomeReviewsGene locus MSMEG_3461 in contig CP000480_GR.
KEGGmsm:MSMEG_3461.
NMPDRfig|246196.1.peg.3467.
TIGRMSMEG_3461.

Phylogenomic databases

OMAFEWELTK.

Family and domain databases

HAMAPMF_01961.
[Tree]
InterProIPR000763. Catalase_proxase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[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 nameKATG2_MYCS2
AccessionPrimary (citable) accession number: A0QXX7
Secondary accession number(s): Q93JZ3, Q9R4J9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: January 9, 2007
Last modified: November 3, 2009
This is version 26 of the entry and version 1 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