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A5FZM1 (KATG_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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

Short name=CP
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase
Gene names
Name:katG
Ordered Locus Names:Acry_1851
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length728 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 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
   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 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 – 1919 Potential
Chain20 – 728709Catalase-peroxidase HAMAP MF_01961
PRO_0000354708

Sites

Active site971Proton acceptor By similarity
Metal binding2601Iron (heme axial ligand) By similarity
Site931Transition state stabilizer By similarity

Amino acid modifications

Cross-link96 ↔ 219Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-245) By similarity
Cross-link219 ↔ 245Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FZM1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 61E17724CD363C4D

FASTA72878,868
        10         20         30         40         50         60 
MSTEAKCPVT GGATRSSSAG IQSNADWWPN QINLGMLHQH SALSNPMDPD FDYAAEFKTL 

        70         80         90        100        110        120 
DLDAVIADLK ALMTDSQDWW PADFGHYGPL FVRMAWHAAG TYRIGDGRGG AGAGQQRFAP 

       130        140        150        160        170        180 
LNSWPDNANL DKARRLLWPV KQKYGRKISW ADLMVLAGNV ALESMGFKTF GFGAGRVDTW 

       190        200        210        220        230        240 
EPDQGIYWGP ETTWLDDKRY SGDRDLENPL AAVQMGLIYV NPEGPNGKPD PVAAARDIRE 

       250        260        270        280        290        300 
TFARMAMNDE ETVALIAGGH TFGKTHGAGD AALVGPEPEA APIEQQGLGW ISSYGTGKGS 

       310        320        330        340        350        360 
DAITGGPEVT WTQTPTQWSN FYFDNLFNYE WELTKSPAGA WQWVAKDAGD VIPDAFDAAK 

       370        380        390        400        410        420 
KHRPTMLTTD LSMRMDPAYE KISRRFHQNP DEFADAFARA WFKLTHRDMG PVSRYLGKLV 

       430        440        450        460        470        480 
PAEHLIWQDP VPAVDHKLID AADIAALKAK LLATGIAPTR LALTAWASAA TFRGSDKRGG 

       490        500        510        520        530        540 
ANGARIRLAP QKDWAANEPA ELAKVLAALE KVQAEFNAAA TGGKKVSLAD LIVLGGCAAI 

       550        560        570        580        590        600 
EAAAKAAGHD VTVPFTPGRT DATEAQTDVA SFAVLEPKAD GFRNYLGKGD PRAPEEQLID 

       610        620        630        640        650        660 
RAQLMTLTAP EMTALIGGMR ALGANVGGAK HGVFTTRPGA LTNDFFVNLL DMNMSWHPAA 

       670        680        690        700        710        720 
EPGVYELRDR KSGAVKWTAT RVDLVFGSNS QLRALAEVYG TQDGEAAFVK DFVAAWTKVM 


ELDRFDLA 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
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., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ31053.1.
RefSeqYP_001234972.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FZM1.
SMRA5FZM1. Positions 23-728.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FZM1.

Protein family/group databases

PeroxiBase3597. AcrCP01_JF-5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5159721.
GenomeReviewsGene locus Acry_1851 in contig CP000697_GR.
KEGGacr:Acry_1851.
PATRIC20648746. VBIAciCry6074_2346.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHBG285610.
OMAKRHAPSM.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycACRY349163:ACRY_1851-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]
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. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_ACICJ
AccessionPrimary (citable) accession number: A5FZM1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 36 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