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Protein

Catalase-peroxidase

Gene

katG

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
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
Sitei95 – 951Transition state stabilizerUniRule annotation
Active sitei99 – 991Proton acceptorUniRule annotation
Metal bindingi263 – 2631Iron (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

BioCyciBHAL272558:GJC5-964-MONOMER.

Protein family/group databases

PeroxiBasei2372. BhaCP01_C-125.

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:BH0906
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Catalase-peroxidasePRO_0000354724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki98 ↔ 222Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248)UniRule annotation
Cross-linki222 ↔ 248Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98)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

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi272558.BH0906.

Structurei

3D structure databases

ProteinModelPortaliQ9KEE6.
SMRiQ9KEE6. Positions 22-724.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KEE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTNNTGKCP FHHGATTSPK SSGTTNNDWW PNALNLNILR QHDKKSNPMG
60 70 80 90 100
EEFDYAEEFS KLDYDALKQD VRDLMRDSQD WWPADFGHYG PFFIRMSWHA
110 120 130 140 150
AGTYRIGDGR GGGGTGNQRF APLNSWPDNG NLDKARRLLW PIKQKYGNKI
160 170 180 190 200
SWADLLVLAG NVAIEDMGGP VIGFGAGRED IWHPEEDIYW GSEKEWLTGD
210 220 230 240 250
KRYSGDRELE NPLAAVEMGL IYVNPEGPDG KPDPIKAAHD IRETFGRMGM
260 270 280 290 300
NDEETVALIA GGHTFGKAHG AGNPDHVGPE PEAAPIEAQG LGWQNTYGSG
310 320 330 340 350
KGRDTITSGL EGAWTANPTQ WDNGFFDLLF GYEWWLTKSP AGAYQWQAVD
360 370 380 390 400
PDEKDLAPDA EDPSVKVPTV MLTTDLALRH DPEYEKISRR FHKNPDEFAD
410 420 430 440 450
AFARAWFKLL HRDMGPKARY LGPEVPAEDF IWQDPVPTVD YELTDAEVEE
460 470 480 490 500
LKAKILDSGL TVSELVTTAW ASASTFRNSD KRGGANGARI RLAPQKDWEV
510 520 530 540 550
NQPEQLEKVL SVLENIQSQL DKKVSIADLI VLGGSAAVEK AAKEAGFDVT
560 570 580 590 600
VPFAPGRGDA TQEQTDVEGF AVLEPVSDGF RNYQKKEYSV SPEELLIDKA
610 620 630 640 650
QLLDLTAPEM TALIGGMRAL GANYGGTQHG VFTDCVGTLT NDFFVNLLDM
660 670 680 690 700
GIEWKPVDYN LYEGRDRKTG EVVRTATRVD LVFGSNSILR AIAEVYAQDD
710 720 730
NKGKFVEDFI AAWVKVMNAD RFDLKLNKKA QLTSK
Length:735
Mass (Da):81,531
Last modified:October 1, 2000 - v1
Checksum:iE93B4B5EBFA3A593
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04625.1.
PIRiB83763.
RefSeqiWP_010897079.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB04625; BAB04625; BAB04625.
KEGGibha:BH0906.
PATRICi18938828. VBIBacHal18977_0952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04625.1.
PIRiB83763.
RefSeqiWP_010897079.1. NC_002570.2.

3D structure databases

ProteinModelPortaliQ9KEE6.
SMRiQ9KEE6. Positions 22-724.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH0906.

Protein family/group databases

PeroxiBasei2372. BhaCP01_C-125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB04625; BAB04625; BAB04625.
KEGGibha:BH0906.
PATRICi18938828. VBIBacHal18977_0952.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-964-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Entry informationi

Entry nameiKATG_BACHD
AccessioniPrimary (citable) accession number: Q9KEE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2000
Last modified: January 20, 2016
This is version 96 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.