Skip Header

Contribute Send feedback
Read comments (?) or add your own

A6TV07 (KATG2_ALKMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catalase-peroxidase 2

Short name=CP 2
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase 2
Gene names
Name:katG2
Ordered Locus Names:Amet_3934
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceUncertain

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.

Caution

Could be the product of a pseudogene. The N-terminus is much shorter than in related proteins and lacks the active sites and the heme-binding sites. Moreover, the 71 first amino acids of this sequence are not homologous to other katG sequences.

Ontologies

Keywords
   Biological processHydrogen peroxide
   DomainSignal
   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 functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 416396Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000354719

Sequences

Sequence LengthMass (Da)Tools
A6TV07 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 01ACF81E6638AD38

FASTA41646,834
        10         20         30         40         50         60 
MLLPLIVFLL SVLIHHRIYS SFFLHFYSPQ YYMICSRLTL LSSCSWHDFH LKLILLEFAS 

        70         80         90        100        110        120 
QSTNPVPALH NDPTYEKISR RFHENPEAFA DVFARAWFKL LHRDMGPQTR YLGPEVPEEE 

       130        140        150        160        170        180 
LIWQDPIPAV DYELTDAEIA ELKAKILDSG LTVSDLVTTA WASASTFRGS DMRGGANGAR 

       190        200        210        220        230        240 
IRLAPQKDWE VNQPEQLTKV LTVLEDIQNQ LDKKVSIADL IVLGGSAAIE KSAQDAGFDV 

       250        260        270        280        290        300 
TVPFALGRGD ATQEQTDIES FEVLEPISDG FRNYQKKQYS VSAEELLLDK AQLLNLTAPE 

       310        320        330        340        350        360 
MTVLVDGMRV LGTNYNGTQH GVFTDRVGTL TNDFFVNLLD MGVEWKPMDG GLYEARNRKT 

       370        380        390        400        410 
GEVVRTATRV DLVFGSNSVL RALVEVYAQD DNKEKFVGDF IAAWIKVMNA DRFDLD 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QYMF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000724 Genomic DNA. Translation: ABR50025.1.
RefSeqYP_001321684.1. NC_009633.1.

3D structure databases

ProteinModelPortalA6TV07.
SMRA6TV07. Positions 68-415.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6TV07.

Protein family/group databases

PeroxiBase3625. AmeCP02_QYMF.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5314015.
GenomeReviewsGene locus Amet_3934 in contig CP000724_GR.
KEGGamt:Amet_3934.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
OMAHHRIYSS.

Enzyme and pathway databases

BioCycAMET293826:AMET_3934-MONOMER.

Family and domain databases

HAMAPMF_01961. Catal-peroxid. Divergent sequence.
[Tree]
InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]
KOK03782.
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
SUPFAMSSF48113. Peroxidase_super. 2 hits.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. False negative.
PS50873. PEROXIDASE_4. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG2_ALKMQ
AccessionPrimary (citable) accession number: A6TV07
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: August 21, 2007
Last modified: November 16, 2011
This is version 30 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