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Q7BSW8 (KATG2_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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 2

Short name=CP 2
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase 2
Gene names
Name:katG2
Synonyms:katP
Ordered Locus Names:L7017, ECO57PM75
Encoded onPlasmid pO157 Ref.1 Ref.2 Ref.3
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Ref.1

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

Subcellular location

Periplasm Ref.1.

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
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Signal peptide1 – 2323 Potential
Chain24 – 736713Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000354782

Sites

Active site1031Proton acceptor By similarity
Metal binding2641Iron (heme axial ligand) By similarity
Site991Transition state stabilizer By similarity

Amino acid modifications

Cross-link102 ↔ 223Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249) By similarity
Cross-link223 ↔ 249Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-102) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7BSW8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F3EA593D3FDEDB8D

FASTA73681,794
        10         20         30         40         50         60 
MIKKTLPVLI LLALSGSFST AVAADKKETQ NFYYPETLDL TPLRLHSPES NPWGADFDYA 

        70         80         90        100        110        120 
TRFQQLDMEA LKKDIKDLLT TSQDWWPADY GHYGPFFIRM AWHGAGTYRT YDGRGGASGG 

       130        140        150        160        170        180 
QQRFEPLNSW PDNVNLDKAR RLLWPVKKKY GSSISWGDLM VLTGNVALES MGFKTLGFAG 

       190        200        210        220        230        240 
GREDDWESDL VYWGPDNKPL ADNRDKNGKL QKPLAATQMG LIYVNPEGPG GKPDPLASAK 

       250        260        270        280        290        300 
DIREAFSRMA MDDEETVALI AGGHTFGKAH GAASPEKCIG AGPDGAPVEE QGLGWKNKCG 

       310        320        330        340        350        360 
TGNGKYTITS GLEGAWSTSP TQFTMQYLKN LYKYEWELHK SPAGAYQWKP KKAANIVQDA 

       370        380        390        400        410        420 
HDPSVLHPLM MFTTDIALKV DPEYKKITTR FLNDPKAFEQ AFARAWFKLT HRDMGPAARY 

       430        440        450        460        470        480 
LGNEVPAESF IWQDPLPAAD YTMIDGKDIK SLKEQVMDLG IPASELIKTA WASASTFRVT 

       490        500        510        520        530        540 
DYRGGNNGAR IRLQPEINWE VNEPEKLKKV LASLTSLQRE FNKKQSDGKK VSLADLIVLS 

       550        560        570        580        590        600 
GNAAIEDAAR KAGVELEIPF TPGRTDASQE QTDVASFSVL EPTADGFRNY YSKSRSHISP 

       610        620        630        640        650        660 
VESLIDKASQ LDLTVPEMTA LLGGLRVMDI NTNNSSLGVF TDTPGVLDNK FFVNLLDMST 

       670        680        690        700        710        720 
RWSKADKEDT YNGFDRKTGA LKWKASSVDL IFSSNPELRA VAEVYASDDA RNKFIHDFVK 

       730 
SWNKVMNSDR FDLNNK 

« Hide

References

« Hide 'large scale' references
[1]"KatP, a novel catalase-peroxidase encoded by the large plasmid of enterohaemorrhagic Escherichia coli O157:H7."
Brunder W., Schmidt H., Karch H.
Microbiology 142:3305-3315(1996) [PubMed: 8969527] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"The complete DNA sequence and analysis of the large virulence plasmid of Escherichia coli O157:H7."
Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J., Blattner F.R.
Nucleic Acids Res. 26:4196-4204(1998) [PubMed: 9722640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]"Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak."
Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C., Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G., Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.
DNA Res. 5:1-9(1998) [PubMed: 9628576] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89017 Genomic DNA. Translation: CAA61429.1.
AF074613 Genomic DNA. Translation: AAC70085.1.
AB011549 Genomic DNA. Translation: BAA31832.1.
PIRT00313.
RefSeqYP_002756743.1. NC_012487.1.
YP_325577.1. NC_007414.1.

3D structure databases

HSSPHSSP built from PDB template 1ITK based on UniProtKB O59651.
ProteinModelPortalQ7BSW8.
SMRQ7BSW8. Positions 33-733.
ModBaseSearch...

Protein family/group databases

PeroxiBase2386. EcoH7CP02_EDL933.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000029387; EBESCP00000028092; EBESCG00000028437.
EBESCT00000060752; EBESCP00000058396; EBESCG00000059799.
GeneID3683716.
7701572.
GenomeReviewsGene locus ECO57PM75 in contig AB011549_GR.
Gene locus L7017 in contig AF074613_GR.
KEGGece:L7017.
PATRIC18360409. VBIEscCol44059_5606.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011618.
HOGENOMHBG285610.
OMAKNKCGKG.
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 nameKATG2_ECO57
AccessionPrimary (citable) accession number: Q7BSW8
Secondary accession number(s): P77038
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 55 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