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Protein

Catalase-peroxidase

Gene

katG

Organism
Shewanella baltica (strain OS195)
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

BioCyciSBAL399599:GH6B-3735-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:Sbal195_3612
OrganismiShewanella baltica (strain OS195)
Taxonomic identifieri399599 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000770 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Catalase-peroxidasePRO_0000354916Add
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

ProteinModelPortaliA9L1H8.
SMRiA9L1H8. Positions 14-720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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.

A9L1H8-1 [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 ISWADLIVLT
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 LFENPDEFAE IFAKAWYKLT
410 420 430 440 450
HRDMGPCTRY LGPEVPAEEF 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 SKTGVFTARP EFLTNDFFVN LLDMGTTWKP
660 670 680 690 700
TSKAEDRFEG VDRVSGQPKW TASRVDLIFG SNSQLRALAE VYASSDAQLR
710 720
FIDDFIAAWT KVMNLDRFDL R
Length:721
Mass (Da):79,524
Last modified:February 5, 2008 - v1
Checksum:i0E16C8CB26A3DE5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000891 Genomic DNA. Translation: ABX50774.1.
RefSeqiWP_006083983.1. NC_009997.1.

Genome annotation databases

EnsemblBacteriaiABX50774; ABX50774; Sbal195_3612.
GeneIDi11773645.
KEGGisbn:Sbal195_3612.
sbt:Sbal678_3635.
PATRICi23473619. VBISheBal33754_3744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000891 Genomic DNA. Translation: ABX50774.1.
RefSeqiWP_006083983.1. NC_009997.1.

3D structure databases

ProteinModelPortaliA9L1H8.
SMRiA9L1H8. Positions 14-720.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX50774; ABX50774; Sbal195_3612.
GeneIDi11773645.
KEGGisbn:Sbal195_3612.
sbt:Sbal678_3635.
PATRICi23473619. VBISheBal33754_3744.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciSBAL399599:GH6B-3735-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OS195.

Entry informationi

Entry nameiKATG_SHEB9
AccessioniPrimary (citable) accession number: A9L1H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 5, 2008
Last modified: March 16, 2016
This is version 54 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

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.