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Reviewed, UniProtKB/Swiss-Prot A1T9D9 (KATG2_MYCVP)

Last modified February 9, 2010. Version 25. 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
Ordered Locus Names: Mvan_2984
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. HAMAP MF_01961

Catalytic activity

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

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

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. HAMAP MF_01961

Subunit structure

Homodimer or homotetramer By similarity. HAMAP MF_01961

Post-translational modification

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961

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: HAMAP

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 737737Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000354848

Sites

Active site1081Proton acceptor By similarity
Metal binding2761Iron (heme axial ligand) By similarity
Site1041Transition state stabilizer By similarity

Amino acid modifications

Cross-link107 ↔ 235Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-261) By similarity
Cross-link235 ↔ 261Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1T9D9-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D628D8A6B2FA46F3

FASTA73780,850
        10         20         30         40         50         60 
MPEATEHPPI GEAQTEPAQS GCPMVIKPPV EGGSNRDWWP NAVNLKMLQK DPEVIDPMDE 

        70         80         90        100        110        120 
GYDYREAVQT LDVDQLARDF DELCTNSQDW WPADFGHYGP LFIRMSWHAA GTYRVQDGRG 

       130        140        150        160        170        180 
GAGKGMQRFA PLNSWPDNVS LDKARRLLWP LKKKYGKKLS WSDLIVYAGN RAMENMGFKT 

       190        200        210        220        230        240 
AGFAFGRPDY WEPEEDVYWG AEHEWLGSQD RYAGANGDRT KLENPLGASH MGLIYVNPEG 

       250        260        270        280        290        300 
PEGNPDPIAA AIDIRETFGR MAMNDVETAA LIVGGHTFGK THGATDIVNG PEPEAAPLEQ 

       310        320        330        340        350        360 
MGLGWSNPGV GIDTVSSGLE VTWTHTPTKW DNSFLEILYG NEWELFKSPA GANQWRPKDN 

       370        380        390        400        410        420 
GWANSVPMAQ GTGKTHPAML TTDLSMRMDP IYGEITRRWL DHPEELAEEY AKAWFKLLHR 

       430        440        450        460        470        480 
DMGPVQRYLG PLVPTQTWLW QDIVPAGKPL SDADVATLKG AIADSGLTVQ QLVSTAWKAA 

       490        500        510        520        530        540 
SSFRISDMRG GANGGRIRLQ PQLGWESNEP DELAQVISKL EEIQGSSGID VSFADLVVLG 

       550        560        570        580        590        600 
GNVGIETAAK AAGFDIEVPF SSGRGDATQE QTDVEAFSYL EPKADGFRNY VGKGLNLPAE 

       610        620        630        640        650        660 
YQLIDQANLL NLSAPQMTVL IGGLRALGIT HGDSKLGVLT DTPGQLTNDY FVNLTDMGVK 

       670        680        690        700        710        720 
WAPAPADDGT YVGTDRDTGE VKYTASRVDL LFGSNSQLRA LAEVYAEDDS RDKFVKDFVA 

       730 
AWVNVMDADR YDIGKGA 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM13789.1.
RefSeqYP_953795.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1T9D9.

Genome annotation databases

GeneID4645112.
GenomeReviewsGene locus Mvan_2984 in contig CP000511_GR.
KEGGmva:Mvan_2984.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHBG285610.
OMANGWANSV.
PhylomeDBA1T9D9.

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
[Tree]
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG2_MYCVP
AccessionPrimary (citable) accession number: A1T9D9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 6, 2007
Last modified: February 9, 2010
This is version 25 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