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Protein

Catalase-peroxidase

Gene

katG

Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Sitei204Transition state stabilizerUniRule annotation1
Active sitei208Proton acceptorUniRule annotation1
Metal bindingi371Iron (heme axial ligand)UniRule annotation1

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

Protein family/group databases

PeroxiBasei2389. RbaCP01_SH.

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:RB3010
OrganismiRhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
Proteomesi
  • UP000001025 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003548911 – 857Catalase-peroxidaseAdd BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki207 ↔ 330Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-356)UniRule annotation
Cross-linki330 ↔ 356Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-207)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

PRIDEiQ7UUW9.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243090.RB3010.

Structurei

3D structure databases

ProteinModelPortaliQ7UUW9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
InParanoidiQ7UUW9.
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.

Q7UUW9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLVHGKDAV NALDVSWLSP ILVRDPTSPS ESAWDLFATF MRTRTMKSTA
60 70 80 90 100
TNMNQHPTTA QICRRFATRL FRGTVSIRPL TLTLGCLAAS ASASLVAQET
110 120 130 140 150
ATNAAASQAD AISKCPVMGN PAGPNRHTVS GAMGNGDWWP NQLNLDMLHQ
160 170 180 190 200
NSVKSNPMGE DFDYAAAFNS LDLAAVKADI KELMNTSQDW WPSDYGHYGP
210 220 230 240 250
LFIRMAWHSA GTYRVSDGRG GASDGTQRFA PLNSWPDNAN LDKARRLLWP
260 270 280 290 300
IKQKYGSKIS WADLMVLTGN CALEDMGFET FGFAGGREDV WEPQKDVYWG
310 320 330 340 350
PETEWLGDKR YSGDRDLQNP LAAVQMGLIY VNPEGPNGKP DPIAAAKDIR
360 370 380 390 400
ETFGRMAMND EETVALIAGG HTFGKAHGAA SPDGNMGVEP EGEGLAAQGL
410 420 430 440 450
GWINTHGTGN AGDTITSGLE GAWTSTPAEW SHGYFENLFG YEWKLVKSPA
460 470 480 490 500
GAWQWTPTDE NAKGTVPDAH DASKSHAPMM FTTDLALRMD PEYGKISRRF
510 520 530 540 550
HDNPEQFEKA FAKAWYKLTH RDMGPVSRLL GDSVPEPQLW QDPIPEATFD
560 570 580 590 600
VIGSKEIEQL KQKILATNLT SSQLVSTAWA SASTFRNSDM RGGANGARIR
610 620 630 640 650
LAPQKDWEVN EPAELASVLT TLEGVQKEFN ASRKDGKQVS MADLIVLGGC
660 670 680 690 700
AGVEAAAMKA GHAIQVPFTP GRTDATQEMT DVESFEPLKP IADGFRNYQG
710 720 730 740 750
HNADRPAEEM LVDKANLLSL TAPEMTVLVG GMRALDTNAG AGPLADLGKL
760 770 780 790 800
TKRPGALTND FFVNLLDMNT VWKQSPMCEH FFEGRDRESG NLKWTASRVD
810 820 830 840 850
LVFGSNSQLR GIAEVYASED AKEKFVKDFV NAWTKVMNLD RFDVNDSEST

ETQVAAK
Length:857
Mass (Da):93,632
Last modified:October 1, 2003 - v1
Checksum:iF28CF3153C2D7330
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294138 Genomic DNA. Translation: CAD72958.1.
RefSeqiNP_865274.1. NC_005027.1.
WP_011119144.1. NC_005027.1.

Genome annotation databases

EnsemblBacteriaiCAD72958; CAD72958; RB3010.
GeneIDi1793861.
KEGGirba:RB3010.
PATRICi23244217. VBIRhoBal59814_1394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294138 Genomic DNA. Translation: CAD72958.1.
RefSeqiNP_865274.1. NC_005027.1.
WP_011119144.1. NC_005027.1.

3D structure databases

ProteinModelPortaliQ7UUW9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243090.RB3010.

Protein family/group databases

PeroxiBasei2389. RbaCP01_SH.

Proteomic databases

PRIDEiQ7UUW9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD72958; CAD72958; RB3010.
GeneIDi1793861.
KEGGirba:RB3010.
PATRICi23244217. VBIRhoBal59814_1394.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
InParanoidiQ7UUW9.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiKATG_RHOBA
AccessioniPrimary (citable) accession number: Q7UUW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2003
Last modified: October 5, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Differs from other KatG proteins because it has a much longer N-terminus.Curated

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.