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Protein

Catalase-peroxidase

Gene

katG

Organism
Shewanella baltica (strain OS185)
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
Sitei86 – 861Transition state stabilizerUniRule annotation
Active sitei90 – 901Proton acceptorUniRule annotation
Metal bindingi253 – 2531Iron (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

BioCyciSBAL402882:GJ99-3609-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:Shew185_3489
OrganismiShewanella baltica (strain OS185)
Taxonomic identifieri402882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723Catalase-peroxidasePRO_0000354915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki89 ↔ 212Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-238)UniRule annotation
Cross-linki212 ↔ 238Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-89)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

Structurei

3D structure databases

ProteinModelPortaliA6WS27.
SMRiA6WS27. Positions 14-720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.

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.

A6WS27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENKCPMHH SAGGTTNRDW WPKQLRLDIL HQHSSLSNPM GDDFNYAEAF
60 70 80 90 100
KSLDLAAVKQ DLLALMTDSQ DWWPADFGHY GPLFIRMAWH SAGTYRTGDG
110 120 130 140 150
RGGAGSGNQR FAPLNSWPDN VSLDKARRLI WPIKQKYGNK ISWADLIILT
160 170 180 190 200
GNVALESMGF KTLGFAGGRV DIWEPEADIY WGAEDKWLDD KRYSGERDLE
210 220 230 240 250
DPLAAVQMGL IYVNPEGPNG DPDPFAAAVD IRETFARMAM NDEETVALIA
260 270 280 290 300
GGHTFGKTHG AGDAALVGPE PEAASIEQQG LGWKSSYKSG KGGDAISSGL
310 320 330 340 350
EVTWTSTPTQ WSNNFFENLF GYEWELTKSP AGAHQWIPKN GAGKGVIPDA
360 370 380 390 400
HDASKRHVPA MLTTDLALIF DPDYEKISRR FFEHPDEFAD VFAKAWYKLT
410 420 430 440 450
HRDMGPCTRY LGPEVPAEAF LWQDPIPAVD HPLVDEQDVT DLKLKIIGSG
460 470 480 490 500
LTISEVVATA WASASTYRGS DMRGGANGAR IRLAPQKDWP VNQPEQLAKV
510 520 530 540 550
LKVLESIQSE FNKSGKKISL ADLIVLAGCV GIDQAARNAG VEVTIPFTPG
560 570 580 590 600
RMDATQAQTD VESFAVLEPV ADGFRNYHPT QFSVSAEELL VDRAQLLTLT
610 620 630 640 650
APEMTVLIGG LRVLDTNADQ SKTGVLTARP EFLTNDFFVN LLDMGTTWKP
660 670 680 690 700
TSKAEDRFEG VDRVSGQPKW TASRVDLIFG SNSQLRALAE VYASSDAQLR
710 720
FIDDFIAAWT KVMNLDRFDL RRA
Length:723
Mass (Da):79,703
Last modified:August 21, 2007 - v1
Checksum:i73858067C2667FD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS09616.1.
RefSeqiWP_012090075.1. NC_009665.1.

Genome annotation databases

EnsemblBacteriaiABS09616; ABS09616; Shew185_3489.
KEGGisbm:Shew185_3489.
PATRICi23464019. VBISheBal127872_3756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS09616.1.
RefSeqiWP_012090075.1. NC_009665.1.

3D structure databases

ProteinModelPortaliA6WS27.
SMRiA6WS27. Positions 14-720.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS09616; ABS09616; Shew185_3489.
KEGGisbm:Shew185_3489.
PATRICi23464019. VBISheBal127872_3756.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.

Enzyme and pathway databases

BioCyciSBAL402882:GJ99-3609-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_SHEB8
AccessioniPrimary (citable) accession number: A6WS27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: August 21, 2007
Last modified: September 7, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.