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A8LTG4 (KATG_DINSH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:Dshi_3801
Encoded onPlasmid pDSHI02
OrganismDinoroseobacter shibae (strain DFL 12) [Complete proteome] [HAMAP]
Taxonomic identifier398580 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeDinoroseobacter

Protein attributes

Sequence length725 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
Plasmid
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 – 725725Catalase-peroxidase HAMAP MF_01961
PRO_0000354769

Sites

Active site991Proton acceptor By similarity
Metal binding2671Iron (heme axial ligand) By similarity
Site951Transition state stabilizer By similarity

Amino acid modifications

Cross-link98 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252) By similarity
Cross-link226 ↔ 252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LTG4 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: EF855E21EAE8FEA2

FASTA72579,174
        10         20         30         40         50         60 
MDGNDLRNVT GCPVMHGGNT GMNTSPVRWW PNALNLDILH QHGARVSPMD PDYDHREAVK 

        70         80         90        100        110        120 
ALDFQGVWDD VDKLLTDSQD WWPADWGHYG GLFIRLSWHA AGSYRLGDGR GGAGTGNLRF 

       130        140        150        160        170        180 
EPLNSWPDNA SLEKARRLLW PVKKKYGNAL SWADLLVLAG TVAYSNMGLK TFGFAFGRKD 

       190        200        210        220        230        240 
IWGPEIDINW GSDSEILAPT DERVTDVADA NSMANPLAAS HMGLIYVNPE GVNGTPDPAQ 

       250        260        270        280        290        300 
TAKYVRMTFA RMAMNDEETA ALTVGGHTVG KAHGGTMADK VGADPAGCPV HMQGFGWENP 

       310        320        330        340        350        360 
GFDGNANTAH TSGLEGAWTS NPTQWDNGYL ELLFKYDWEV TKSRAGAFQW EPVNIAEEDM 

       370        380        390        400        410        420 
VPDATDPSIK HNPIMTDADM AMKVDPIYRE ICERFHKDPD YLADTFARAW FKLTHRDMGP 

       430        440        450        460        470        480 
KANYYGPFVP QEDLIWQDPI PEGPTGYDVD ALKAKIAESG LSAAEMIATA WDSARTFRGS 

       490        500        510        520        530        540 
DMRGGANGAR IRLVPQKDWA GNEPERLAKV LGILEPLAAA AGASIADTIV LAGNVGIEMA 

       550        560        570        580        590        600 
IKAAGQDVPV PFAPGRGDAT DAMTDAESFE VMEPFADGFR NWSKERYSVS PEELMLDRAQ 

       610        620        630        640        650        660 
LLGLTAAEMA VLVGGLRVLG ANHGGSAHGV FTDRVGTLTT DFFQTITDMA YKWVPLDDGT 

       670        680        690        700        710        720 
YEIRDRKSGD TVYTATSADL VFGSNSQLRA IAEVYAQDDN ETKFVRDFVA AWTKVMNADR 


FDLLA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000832 Genomic DNA. Translation: ABV95531.1.
RefSeqYP_001542012.1. NC_009956.1.

3D structure databases

ProteinModelPortalA8LTG4.
SMRA8LTG4. Positions 25-723.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8LTG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5714330.
GenomeReviewsGene locus Dshi_3801 in contig CP000832_GR.
KEGGdsh:Dshi_3801.
PATRIC21820415. VBIDinShi9476_3934.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG285610.
OMAWPNALNL.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycDSHI398580:DSHI_3801-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.
[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. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_DINSH
AccessionPrimary (citable) accession number: A8LTG4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 32 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