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Protein

Catalase-peroxidase

Gene

katG

Organism
Ralstonia pickettii (strain 12J)
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

BioCyciRPIC402626:GH94-2961-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:Rpic_2922
OrganismiRalstonia pickettii (strain 12J)
Taxonomic identifieri402626 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
Proteomesi
  • UP000002566 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515UniRule annotationAdd
BLAST
Chaini16 – 721706Catalase-peroxidasePRO_0000354879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki98 ↔ 221Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248)UniRule annotation
Cross-linki221 ↔ 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

Proteomic databases

PRIDEiB2UBU5.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi402626.Rpic_2922.

Structurei

3D structure databases

ProteinModelPortaliB2UBU5.
SMRiB2UBU5. Positions 23-719.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

B2UBU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEAKCPFS GHAPAASHAF GGGTANKDWW PNQLRVDLLN QHSEKSDPLG
60 70 80 90 100
SNFNYRKSFN AIDYDALKAD LRRLMTDSQD WWPADFGHYG PQFIRMAWHA
110 120 130 140 150
AGTYRTGDGR GGAGRGQQRF APLNSWPDNV NIDKSRRLLW PIKQKYGQAI
160 170 180 190 200
SWADLLILTG NVALETMGFR TFGFAAGRED TWEPDNDVYW GNETKWLEAT
210 220 230 240 250
RYSGERNLAN PLAAVQMGLI YVNPEGPEHA HGDPLAAAKD IRETFARMAM
260 270 280 290 300
DDEETVALIA GGHTFGKTHG AGPASHVGAD VEAAPLEAQG LGWASTFGTG
310 320 330 340 350
KGADAITSGL EVTWTQTPAQ WSNFFFENLF KYEWVQEKSP AGALQWVAKD
360 370 380 390 400
AEAIIPGPTP DSPKRRPTML TTDLSLRFDP AYEKISRRFL DNPQAFAEAF
410 420 430 440 450
ARAWFKLTHR DLGPKSRYLG PEVPREDLIW QDPLPTATHK PTEADIADLK
460 470 480 490 500
AKIAASGLSA SELVAVAWAS ASTFRGSDKR GGANGARIRL APQKDWAVNQ
510 520 530 540 550
PVAGTLARLE EIQRASGKAS LADVIVLAGS VGIELAAKAA GTTITVPFTP
560 570 580 590 600
GRVDATAEQT DATSFSVLEP VADGFRNYQK TQFAVPGEVL LLDRAQLLTL
610 620 630 640 650
TAPELTVLIG GLRAININAD GSQHGVFTST PGALTNDFFV NLLDMNTEWK
660 670 680 690 700
PAGDIYEGYD RKTGERKWTG TRVDLVFGSN SILRALAEVF GSADGKERFI
710 720
SEFVAAWVKV MNLDRFDLAA A
Length:721
Mass (Da):78,618
Last modified:July 1, 2008 - v1
Checksum:iA0403F757CE8B853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001068 Genomic DNA. Translation: ACD28045.1.
RefSeqiWP_012436375.1. NC_010682.1.

Genome annotation databases

EnsemblBacteriaiACD28045; ACD28045; Rpic_2922.
GeneIDi6288788.
KEGGirpi:Rpic_2922.
PATRICi20256661. VBIRalPic63053_4063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001068 Genomic DNA. Translation: ACD28045.1.
RefSeqiWP_012436375.1. NC_010682.1.

3D structure databases

ProteinModelPortaliB2UBU5.
SMRiB2UBU5. Positions 23-719.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi402626.Rpic_2922.

Proteomic databases

PRIDEiB2UBU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD28045; ACD28045; Rpic_2922.
GeneIDi6288788.
KEGGirpi:Rpic_2922.
PATRICi20256661. VBIRalPic63053_4063.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciRPIC402626:GH94-2961-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 sequence of chromosome 1 of Ralstonia pickettii 12J."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Marsh T., Richardson P.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12J.

Entry informationi

Entry nameiKATG_RALPJ
AccessioniPrimary (citable) accession number: B2UBU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 1, 2008
Last modified: December 9, 2015
This is version 51 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.