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B2TJE9 (KATG_CLOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase-peroxidase

Short name=CP
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase
Gene names
Name:katG
Ordered Locus Names:CLL_A1367
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length730 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

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

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

Cofactor

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

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

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 730730Catalase-peroxidase HAMAP MF_01961
PRO_0000354764

Sites

Active site961Proton acceptor By similarity
Metal binding2591Iron (heme axial ligand) By similarity
Site921Transition state stabilizer By similarity

Amino acid modifications

Cross-link95 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) By similarity
Cross-link218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-95) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2TJE9 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 0EBD9CB4530E3A38

FASTA73082,089
        10         20         30         40         50         60 
MTENKCPVTG KMGKATAGSG TTNKDWWPNQ LNLNILHQNS QLSNPMSKDF NYAEEFKKLD 

        70         80         90        100        110        120 
FQALKVDLYM LMTDSQIWWP ADYGNYGPLF IRMAWHSAGT YRVGDGRGGG SLGLQRFAPL 

       130        140        150        160        170        180 
NSWPDNINLD KARRLLWPIK KKYGNKISWA DLLILTGNCA LESMGLKTLG FGGGRVDVWE 

       190        200        210        220        230        240 
PQEDIYWGSE KEWLGDEREK GDKELENPLA AVQMGLIYVN PEGPNGNPDP LGSAHDVRET 

       250        260        270        280        290        300 
FARMAMNDEE TVALIAGGHT FGKCHGAASP SYVGPAPEAA PIEEQGLGWK NTYGSGNGDD 

       310        320        330        340        350        360 
TIGSGLEGAW KANPTKWTMG YLKTLFKYDW ELVKSPAGAY QWLAKNVDEE DMVIDAEDST 

       370        380        390        400        410        420 
KKHRPMMTTA DLGLRYDPIY EPIARNYLKN PEKFAHDFAS AWFKLTHRDM GPISRYLGPE 

       430        440        450        460        470        480 
VPKESFIWQD PIPLVKHKLI TKKDITHIKK KILDSGLSIS DLVATAWASA STFRGSDKRG 

       490        500        510        520        530        540 
GANGGRIRLE PQKNWEVNEP KKLNNVLNTL KQIKENFNSS HSKDKKVSLA DIIILGGCVG 

       550        560        570        580        590        600 
IEQAAKRAGY NINVPFIPGR TDAIQEQTDV KSFAVLEPKE DGFRNYLKTK YVVKPEDMLI 

       610        620        630        640        650        660 
DRAQLLTLTA PEMTVLIGGM RVLNCNYNKS KDGVFTNRPE CLTNDFFVNL LDMNTVWKPK 

       670        680        690        700        710        720 
SEDKDRFEGF DRETGELKWT ATRVDLIFGS NSQLRAIAEV YACDDNKEKF IQDFIFAWNK 

       730 
IMNADRFEIK 

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References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Eklund 17B / Type B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001056 Genomic DNA. Translation: ACD21810.1.
RefSeqYP_001885565.1. NC_010674.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2TJE9.

Protein family/group databases

PeroxiBase6254. CboCP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6294293.
GenomeReviewsGene locus CLL_A1367 in contig CP001056_GR.
KEGGcbk:CLL_A1367.
PATRIC19395580. VBICloBot123574_1300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG285610.
OMAKRHAPSM.
ProtClustDBPRK15061.

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]
KOK03782.
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
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_CLOBB
AccessionPrimary (citable) accession number: B2TJE9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families