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Protein

Catalase-peroxidase

Gene

katG

Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
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
Sitei88 – 881Transition state stabilizerUniRule annotation
Active sitei92 – 921Proton acceptorUniRule annotation
Metal bindingi259 – 2591Iron (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

BioCyciBMUL395019:GIYO-578-MONOMER.

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:Bmul_2660, BMULJ_00578
OrganismiBurkholderia multivorans (strain ATCC 17616 / 249)
Taxonomic identifieri395019 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000008815 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728Catalase-peroxidasePRO_0000354745Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki91 ↔ 218Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244)UniRule annotation
Cross-linki218 ↔ 244Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91)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

STRINGi395019.BMULJ_00578.

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.
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.

A9AGE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEPKCPFH HTAGSGTSNK DWWPNQINLN ILHRHSSLSD PMDKDFNYAE
60 70 80 90 100
AFKQLDLAAV KRDLHALMTT SQDWWPADFG HYGGLFIRMA WHSAGTYRIA
110 120 130 140 150
DGRGGAGGGQ QRFAPLNSWP DNANLDKARR LLWPIKQKYG RNISWADLLI
160 170 180 190 200
LTGNVALESM GFKTFGYAGG RPDTWEPDDV YWGSEKIWLE LSGGPNSRYS
210 220 230 240 250
GNRELENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRET FARMAMNDEE
260 270 280 290 300
TVALIAGGHT FGKTHGAGPA SSVGPEPEAA ALEQQGLGWQ STFGTGKGKD
310 320 330 340 350
AITSGLEVTW TSTPTKWSND FFKHLFSYEW ELTKSPAGAH QWVAKDAEAV
360 370 380 390 400
IPDAFDPSKK HRPTMLTTDL ALRFDPEYEK ISRRFYEHPD QFADAFARAW
410 420 430 440 450
FKLTHRDMGP RSRYLGPDVP AEELLWQDPV PAVDHPLIDE ADIAALKAKV
460 470 480 490 500
LASGLSVSQL VSTAWASAST FRGSDKRGGA NGARIRLAPQ KDWEVNRPAE
510 520 530 540 550
LAAVLETLEG VRKAFNDAQT GGKRVSLADL IVLAGAAGVE QAAKNAGVAV
560 570 580 590 600
TVPFAPGRTD ASQEQTDVHA MAVLEPVADG FRNYLKRKFK TPAEALLVDK
610 620 630 640 650
AQLLTLTAPE MTVLVGGMRV LGTNVGDPKH GVFTERPGTL TNDFFVNLLD
660 670 680 690 700
MRTEWKPASA DNDVFEGRDR ATGELKWTGT RVDLVFGSHS QLRALAEVYG
710 720
SADAQQKFVH DFVAAWNKVM NLDRFDLV
Length:728
Mass (Da):79,942
Last modified:November 25, 2008 - v2
Checksum:i8E1446EC9B268E5B
GO

Sequence cautioni

The sequence ABX16344 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000868 Genomic DNA. Translation: ABX16344.1. Different initiation.
AP009385 Genomic DNA. Translation: BAG42542.1.
RefSeqiWP_012467484.1. NC_010804.1.

Genome annotation databases

EnsemblBacteriaiABX16344; ABX16344; Bmul_2660.
BAG42542; BAG42542; BMULJ_00578.
KEGGibmj:BMULJ_00578.
bmu:Bmul_2660.
PATRICi19162863. VBIBurMul203716_1531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000868 Genomic DNA. Translation: ABX16344.1. Different initiation.
AP009385 Genomic DNA. Translation: BAG42542.1.
RefSeqiWP_012467484.1. NC_010804.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi395019.BMULJ_00578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX16344; ABX16344; Bmul_2660.
BAG42542; BAG42542; BMULJ_00578.
KEGGibmj:BMULJ_00578.
bmu:Bmul_2660.
PATRICi19162863. VBIBurMul203716_1531.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciBMUL395019:GIYO-578-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.
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...

Entry informationi

Entry nameiKATG_BURM1
AccessioniPrimary (citable) accession number: A9AGE5
Secondary accession number(s): B3CXN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: September 7, 2016
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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.