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Reviewed, UniProtKB/Swiss-Prot Q7A978 (KATG1_ECO57)

Last modified February 9, 2010. Version 44. 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

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Names and origin

Protein namesRecommended name:
    Catalase-peroxidase 1
      Short name=CP 1
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 1
Gene names
Name: katG1
Ordered Locus Names: Z5497, ECs4871
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length726 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 726726Catalase-peroxidase 1 HAMAP MF_01961
PRO_0000354781

Sites

Active site1061Proton acceptor By similarity
Metal binding2671Iron (heme axial ligand) By similarity
Site1021Transition state stabilizer By similarity

Amino acid modifications

Cross-link105 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252) By similarity
Cross-link226 ↔ 252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105) By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q7A978-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 24D32EA9DEB33A06

FASTA72680,040
        10         20         30         40         50         60 
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF 

        70         80         90        100        110        120 
DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA 

       130        140        150        160        170        180 
GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG 

       190        200        210        220        230        240 
FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS 

       250        260        270        280        290        300 
AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST 

       310        320        330        340        350        360 
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP 

       370        380        390        400        410        420 
DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS 

       430        440        450        460        470        480 
RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG 

       490        500        510        520        530        540 
GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA 

       550        560        570        580        590        600 
ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ 

       610        620        630        640        650        660 
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK 

       670        680        690        700        710        720 
ELFEGRDRET GEVKYTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL 


DRFDLL

« Hide

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References

[1]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
[2]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed: 11206551] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000007 Genomic DNA. Translation: BAB38294.1.
AE005174 Genomic DNA. Translation: AAG59143.1.
PIRC86085.
G91237.
RefSeqNP_290579.1.
NP_312898.1.

3D structure databases

HSSPHSSP built from PDB template 1U2L based on UniProtKB P13029.
SMRQ7A978. Positions 30-725.
ModBaseSearch...

Protein family/group databases

PeroxiBase2718. EcoH7CP01_Sakai.

Genome annotation databases

GeneID915019.
960189.
GenomeReviewsGene locus Z5497 in contig AE005174_GR.
Gene locus ECs4871 in contig BA000007_GR.
KEGGece:Z5497.
ecs:ECs4871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG285610.

Enzyme and pathway databases

BioCycECOL83334:ECS4871-MONOMER.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameKATG1_ECO57
AccessionPrimary (citable) accession number: Q7A978
Secondary accession number(s): Q8X765
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 44 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)

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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