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Protein

Catalase-peroxidase

Gene

katG

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.UniRule annotation

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei93 – 931Transition state stabilizerUniRule annotation
Active sitei97 – 971Proton acceptorUniRule annotation
Metal bindingi265 – 2651Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciDARO159087:GI5B-3914-MONOMER.

Protein family/group databases

PeroxiBasei2367. DarCP01_RCB.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:Daro_3836
OrganismiDechloromonas aromatica (strain RCB)
Taxonomic identifieri159087 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
Proteomesi
  • UP000000550 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736Catalase-peroxidasePRO_0000354766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki96 ↔ 224Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-250)UniRule annotation
Cross-linki224 ↔ 250Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96)UniRule annotation

Post-translational modificationi

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

Proteomic databases

PRIDEiQ479B7.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi159087.Daro_3836.

Structurei

3D structure databases

ProteinModelPortaliQ479B7.
SMRiQ479B7. Positions 23-735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q479B7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNEQKCPFS GTHGARTTVG TQSNRDWWPK VLNLNILHQH APAANPMDAD
60 70 80 90 100
FDYSETFKTL DFGALKQDLY ALMTTSQDWW PADWGHYGGL FIRMAWHSAG
110 120 130 140 150
TYRTGDGRGG AGTGNQRFAP INSWPDNGNL DKARRLLWPI KQKYGNKISW
160 170 180 190 200
ADLMILAGNC ALESMGFKTF GFGGGRVDIW QPEEDIYWGA EREWLATSDK
210 220 230 240 250
PNSRYSGERN LDNPLAAVQM GLIYVNPEGP DGNPDPVASG RDIRETFARM
260 270 280 290 300
AMNDEETVAL TAGGHTFGKA HGAGDPALVG PEPEAAPIEE QGLGWINKFG
310 320 330 340 350
SGKGIHATTS GIEGAWKPNP TKWDNGYFDM LFGYEWELTR SPAGAKQWVA
360 370 380 390 400
KDCKPEHLIP DAHDPSKKHP PMMTTADLAM RFDPIYGPIS RRFHQDPAAF
410 420 430 440 450
ADAFARAWFK LTHRDLGPKA RYLGPEVPAE DLVWQDPIPA VDHPLIEVTD
460 470 480 490 500
VASLKAKLLA SGLSTAELVS TAWASASTFR GSDKRGGANG ARIRLAPQKD
510 520 530 540 550
WAANQPAQLA KVLGVLEGIQ QAFNSAQTGG KKVSLADLIV LGGCAAVEAA
560 570 580 590 600
AKAAGFAVAV PFTPGRTDAS QEQTDAESIA VLEPEADGFR NYQKKTYSVS
610 620 630 640 650
AEEMLVDKAQ LLTLSAPEMT VLVGGLRVLG GNVGGSSDGV FTTTPGTLSN
660 670 680 690 700
DFFVNLLDMG TVWKPAAESA GRYEGRDRQT GVAKWTASRV DLIFGSNSQL
710 720 730
RALAEVYAQN DAQEKFVRDF IAAWSKVMEL DRFDLK
Length:736
Mass (Da):80,014
Last modified:September 13, 2005 - v1
Checksum:i7D3C0F3432884025
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ48564.1.
RefSeqiWP_011289559.1. NC_007298.1.

Genome annotation databases

EnsemblBacteriaiAAZ48564; AAZ48564; Daro_3836.
KEGGidar:Daro_3836.
PATRICi21606364. VBIDecAro89105_3822.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ48564.1.
RefSeqiWP_011289559.1. NC_007298.1.

3D structure databases

ProteinModelPortaliQ479B7.
SMRiQ479B7. Positions 23-735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi159087.Daro_3836.

Protein family/group databases

PeroxiBasei2367. DarCP01_RCB.

Proteomic databases

PRIDEiQ479B7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ48564; AAZ48564; Daro_3836.
KEGGidar:Daro_3836.
PATRICi21606364. VBIDecAro89105_3822.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Enzyme and pathway databases

BioCyciDARO159087:GI5B-3914-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKATG_DECAR
AccessioniPrimary (citable) accession number: Q479B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: September 13, 2005
Last modified: September 7, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.