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Protein

Catalase-peroxidase

Gene

katG

Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
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
Sitei99 – 991Transition state stabilizerUniRule annotation
Active sitei103 – 1031Proton acceptorUniRule annotation
Metal bindingi265 – 2651Iron (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

BioCyciSWOO392500:GI2C-4038-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:Swoo_3905
OrganismiShewanella woodyi (strain ATCC 51908 / MS32)
Taxonomic identifieri392500 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002168 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121UniRule annotationAdd
BLAST
Chaini22 – 736715Catalase-peroxidasePRO_5000316507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki102 ↔ 224Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-250)UniRule annotation
Cross-linki224 ↔ 250Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-102)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

PRIDEiB1KFI8.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi392500.Swoo_3905.

Structurei

3D structure databases

ProteinModelPortaliB1KFI8.
SMRiB1KFI8. Positions 29-735.
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.
OMAiVVWTPTP.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. 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.

B1KFI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKKTILSFV ISAVMVTAAS AVENEQPKSN QFWWPNQLDL TPLRNHSDES
60 70 80 90 100
NPQNSNFDYA EAFEKLDLEA VKKDIDKVLT NSQDWWPADY GHYGPFFIRM
110 120 130 140 150
AWHAAGTYRT HDGRGGAGGG QQRFDPLNSW PDNVNLDKAR RLLWPIKQKY
160 170 180 190 200
GQSISWADLI ALTGNVALES MGFKTYGYAG GREDDWEPDL VYWGPESKFL
210 220 230 240 250
TDERRDKKGK LKGPLAAVEM GLIYVNPVGP HGNPDPLLAA NDIRMSFGRM
260 270 280 290 300
AMNDEEIVAL IAGGHTFGKA HGAKKPTECV GPEPAAAAVE EQGFGWKNRC
310 320 330 340 350
GTGSGADTTS SGLEGAWTIT PTQWTTNYLD NLFTFNWVKT KSPAGAIQWI
360 370 380 390 400
PDTDTAANLV PDAHDPTKRH APIMFTTDIA IKEDPKFRAI AESFRKSPDK
410 420 430 440 450
YELAFAKAWF KLNHRDLGPR SRYLGNEVPK EVLVWQDPIP ELNHPVVNDA
460 470 480 490 500
DIAKLKSEIL KSGLSVQDLV LTAWASASSY RGTDMRGGAN GARINLSPQN
510 520 530 540 550
EWQVNNPKQL AKVLNKLEKI KDKFNKKSKK AKISLADLIV LGGAAAIEKS
560 570 580 590 600
VKEAGFNNKV PFTPGRMDAS QAMTDVASFG VLESTADGFR NYYSDESNLS
610 620 630 640 650
PAQMLIDKAD LLTLTVPEMT ALVGGMRALS ANADGSNHGV FTDQPGVLSN
660 670 680 690 700
DFFVNLLDMS VKWSKKPKSE ALYEGYDRKT GKLKWTATPV DLVFGSNTEL
710 720 730
RAISEFYASK NAEEQFITDF IAAWHKVMVN DRFDIK
Length:736
Mass (Da):81,474
Last modified:April 29, 2008 - v1
Checksum:i1E411341E32F9B0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000961 Genomic DNA. Translation: ACA88163.1.
RefSeqiWP_012326493.1. NC_010506.1.

Genome annotation databases

EnsemblBacteriaiACA88163; ACA88163; Swoo_3905.
KEGGiswd:Swoo_3905.
PATRICi23610475. VBISheWoo126588_4023.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000961 Genomic DNA. Translation: ACA88163.1.
RefSeqiWP_012326493.1. NC_010506.1.

3D structure databases

ProteinModelPortaliB1KFI8.
SMRiB1KFI8. Positions 29-735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi392500.Swoo_3905.

Proteomic databases

PRIDEiB1KFI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA88163; ACA88163; Swoo_3905.
KEGGiswd:Swoo_3905.
PATRICi23610475. VBISheWoo126588_4023.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciSWOO392500:GI2C-4038-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51908 / MS32.

Entry informationi

Entry nameiKATG_SHEWM
AccessioniPrimary (citable) accession number: B1KFI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: April 29, 2008
Last modified: December 9, 2015
This is version 56 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.