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Protein

Catalase-peroxidase

Gene

katG

Organism
Desulfococcus oleovorans (strain DSM 6200 / Hxd3)
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
Sitei89 – 891Transition state stabilizerUniRule annotation
Active sitei93 – 931Proton acceptorUniRule annotation
Metal bindingi261 – 2611Iron (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

BioCyciDOLE96561:GHF3-1669-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:Dole_1646
OrganismiDesulfococcus oleovorans (strain DSM 6200 / Hxd3)
Taxonomic identifieri96561 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfococcus
Proteomesi
  • UP000008561 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 732732Catalase-peroxidasePRO_0000354768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki92 ↔ 220Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-246)UniRule annotation
Cross-linki220 ↔ 246Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-92)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

PRIDEiA9A0F0.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi96561.Dole_1646.

Structurei

3D structure databases

ProteinModelPortaliA9A0F0.
SMRiA9A0F0. Positions 17-732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
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.
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.

A9A0F0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKDSKRPVV GSTVRGGMSN RDWWPNQLNL SILHQQSNKS NPMGEDFDYA
60 70 80 90 100
KEFKKLNLAA VKKDLYALMT DSQEWWPADY GHYGGLFIRM AWHSAGTYRM
110 120 130 140 150
GDGRGGAGSG SQRLAPLNSW PDNANLDKAR RLLWPIKKKY GKRISWADLM
160 170 180 190 200
VLAGNCALES MGFKTFGFAG GREDVWEPET DIYWGAEEEW LATSDKPKSR
210 220 230 240 250
YSGDRDLENP LAAVQMGLIY VNPEGPDGNP DPVAAGYDVI ETFARMAMDP
260 270 280 290 300
EETVALVAGG HTFGKCHGAG PASHVGPEPE AAPIEAQGLG WKSSFGTGKG
310 320 330 340 350
GDTITSGIEG AWKPYPTRWD MGYLKVLFKY EWELVKSPAG AYQWLAMDVD
360 370 380 390 400
EEDMVIDAHD PSKKHRPMMT TADLSLRFDP VLGPIAKRFS KNPKAFADAF
410 420 430 440 450
ARAWFKLTHR DMGPRSRYLG PEVPKKELIW QDPVPAVNHK LIGARDIAAL
460 470 480 490 500
KREILASGLS VSQLVYTAWS SAVTFRGSDK RGGANGARIR LAPQKEWEVN
510 520 530 540 550
QPAQLKKVLA KLEKIRRAFN SAQSDGKKVS LADLIVLGGC AAIEQAARNA
560 570 580 590 600
GYKGTVPFKP GRMDATQKQT DAASFAVLEP LADGFRNYLK AKFTVSAEEL
610 620 630 640 650
LIDKARLLTL TAPEMTVLIG GMRVLNANYG QSPHGVFTKR PETLTNDFFV
660 670 680 690 700
NLLDMGTVWN PAKADDCVFE GRDRQTGALR WTGTRVDLLF GSNSQLRAIA
710 720 730
EVYACKDAGE KFVNDFVAVW NKVMNADRFD LA
Length:732
Mass (Da):80,818
Last modified:January 15, 2008 - v1
Checksum:i7E7AFB4F8E5A2558
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000859 Genomic DNA. Translation: ABW67450.1.
RefSeqiWP_012175066.1. NC_009943.1.

Genome annotation databases

EnsemblBacteriaiABW67450; ABW67450; Dole_1646.
KEGGidol:Dole_1646.
PATRICi21693381. VBIDesOle35880_1698.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000859 Genomic DNA. Translation: ABW67450.1.
RefSeqiWP_012175066.1. NC_009943.1.

3D structure databases

ProteinModelPortaliA9A0F0.
SMRiA9A0F0. Positions 17-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi96561.Dole_1646.

Proteomic databases

PRIDEiA9A0F0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABW67450; ABW67450; Dole_1646.
KEGGidol:Dole_1646.
PATRICi21693381. VBIDesOle35880_1698.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Enzyme and pathway databases

BioCyciDOLE96561:GHF3-1669-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_DESOH
AccessioniPrimary (citable) accession number: A9A0F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: January 15, 2008
Last modified: September 7, 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, 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.