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Protein

Catalase-peroxidase

Gene

katG

Organism
Shewanella sp. (strain W3-18-1)
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
Sitei94 – 941Transition state stabilizerUniRule annotation
Active sitei98 – 981Proton acceptorUniRule annotation
Metal bindingi266 – 2661Iron (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

BioCyciSSP351745:GCOY-280-MONOMER.

Protein family/group databases

PeroxiBasei3623. SHspCP01_W3-18-1.

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:Sputw3181_0269
OrganismiShewanella sp. (strain W3-18-1)
Taxonomic identifieri351745 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728Catalase-peroxidasePRO_0000354927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki97 ↔ 225Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-251)UniRule annotation
Cross-linki225 ↔ 251Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-97)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

ProteinModelPortaliA1REM5.
SMRiA1REM5. Positions 27-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiQPEEMML.
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.
[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.

A1REM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKTHSSQGK CPVMHGGNTS VTTNNMDWWP KALNLDILHQ HDKKTDPMDP
60 70 80 90 100
TFNYSEAFKT LDLAAVKQDL YALMTDSQDW WPADWGHYGG LMIRMAWHSA
110 120 130 140 150
GTYRIADGRG GAGTGNQRFA PLNSWPDNAN LDKARRLLWP IKKKYGNKLS
160 170 180 190 200
WADLIILAGN VAYESMGLKT YGFAGGRADI WHPEKDIYWG SEKQWLAPSD
210 220 230 240 250
NPNSRYSGER DLENPLAAVM MGLIYVNPEG VDGNPDPLRT AQDIRITFAR
260 270 280 290 300
MAMDDEETVA LTAGGHTVGK CHGNGKAQNL GPEPEAEDVE AQGLGWLNKH
310 320 330 340 350
GRGVGRNTVT SGIEGAWTTH PTQWDNGYFS LLLGYDWELK KSPAGAWQWE
360 370 380 390 400
PINIKEEDKP VDVEDPTIRH NPIMTDADMA MKMDPEYRKI SEKFYKDPAY
410 420 430 440 450
FSEVFARAWF KLTHRDLGPK SRYLGPEVPA EDLIWQDPIP QVDYRLSDDD
460 470 480 490 500
ITALKAKILA SGLSIAELVT TAWDSARTFR GSDYRGGANG ARIRLAPQKD
510 520 530 540 550
WEGNEPVRLQ KVLKVLTDIQ TGLSQKVSIA DLIVLGGTAA VEKAAQDAGV
560 570 580 590 600
NIRVPFASGR GDASQEMTDI ESFAVLEPLH DAYRNWQKKD YVVQPEELML
610 620 630 640 650
DRTQLMGLTA HEMTVLIGGM RVLGANYAGS AHGVFTDRVG VLSNDFFVNL
660 670 680 690 700
TDMSYNWKPA GNNLYQIIER KTGTVKWTAT RVDLVFGSNS VLRSYAEIYA
710 720
QDDAKEKFVH DFVNAWTKVM NADRFDLA
Length:728
Mass (Da):81,303
Last modified:February 6, 2007 - v1
Checksum:iD34F34094D910084
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM23120.1.
RefSeqiWP_011787666.1. NC_008750.1.

Genome annotation databases

EnsemblBacteriaiABM23120; ABM23120; Sputw3181_0269.
KEGGishw:Sputw3181_0269.
PATRICi23593927. VBISheSp103602_0277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM23120.1.
RefSeqiWP_011787666.1. NC_008750.1.

3D structure databases

ProteinModelPortaliA1REM5.
SMRiA1REM5. Positions 27-727.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei3623. SHspCP01_W3-18-1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM23120; ABM23120; Sputw3181_0269.
KEGGishw:Sputw3181_0269.
PATRICi23593927. VBISheSp103602_0277.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiQPEEMML.
OrthoDBiPOG091H05R1.

Enzyme and pathway databases

BioCyciSSP351745:GCOY-280-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.
[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...

Entry informationi

Entry nameiKATG_SHESW
AccessioniPrimary (citable) accession number: A1REM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 6, 2007
Last modified: September 7, 2016
This is version 63 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.