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Protein

Catalase-peroxidase

Gene

katG

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.UniRule annotation1 Publication

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
Sitei105 – 1051Transition state stabilizerUniRule annotation
Active sitei109 – 1091Proton acceptorUniRule annotation
Metal bindingi272 – 2721Iron (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

Protein family/group databases

PeroxiBasei2351. ScoCP01_A3.

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
Synonyms:catC, cpeB
Ordered Locus Names:SCO0560
ORF Names:SCF73.07c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Catalase-peroxidasePRO_0000055576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki108 ↔ 231Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257)UniRule annotation
Cross-linki231 ↔ 257Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-108)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

PRIDEiQ9RJH9.

Expressioni

Inductioni

Induced in late exponential growth phase (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi100226.SCO0560.

Structurei

3D structure databases

ProteinModelPortaliQ9RJH9.
SMRiQ9RJH9. Positions 33-740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0376. LUCA.
HOGENOMiHOG000218110.
InParanoidiQ9RJH9.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.
PhylomeDBiQ9RJH9.

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.

Q9RJH9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENHDAIVT DAKTEETDGC PVAHGRAPHP TQGGGNRQWW PERLNLKILA
60 70 80 90 100
KNPAVANPLG EEFDYAEAFE ALDLAAVKRD IAEVLTTSQD WWPADFGNYG
110 120 130 140 150
PLMIRMAWHS AGTYRISDGR GGAGAGQQRF APLNSWPDNG NLDKARRLLW
160 170 180 190 200
PVKKKYGQNL SWADLLVLTG NVALETMGFE TFGFAGGRAD VWEAEEDVYW
210 220 230 240 250
GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN PDPIAAARDI
260 270 280 290 300
RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADAVGDDP EAAAMEQQGL
310 320 330 340 350
GWKSTHGTGK GGDAITSGLE VTWTSTPTQW GNGFFKNLFE FEYELEQSPA
360 370 380 390 400
GANQWVAKDA PEIIPDAHDP AKKHRPRMLT TDLSLRLDPI YGPISRRFYE
410 420 430 440 450
NPEEFADAFA RAWFKLTHRD MGPKSLYLGP EVPEETLIWQ DPLPEPEGEV
460 470 480 490 500
IDAEDVATLK TKLLESGLSV SQLVTTAWAS ASTFRGSDKR GGANGARIRL
510 520 530 540 550
EPQRGWEVNE PDELAQVLRV LEGVQREFNS GSGAKKVSLA DLIVLGGSAA
560 570 580 590 600
VEKAAKEAGF PVEVPFAAGR VDATEEHTDA ESFEALEPTA DGFRNYLGKG
610 620 630 640 650
NRLPAEFLLL DRANLLTLSA PEMTVLVGGL RVLGAGHQQS QLGVFTRTPG
660 670 680 690 700
SLTNDFFVNL LDLGTTWKST SEDRTTFEGR DAATGEVKWA GSRADLVFGS
710 720 730 740
NAELRALAEV YASDDAGEKF VHDFVAAWVK VMNLDRFDLA
Length:740
Mass (Da):80,816
Last modified:May 1, 2000 - v1
Checksum:i767C0A9BC9BD7798
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151D → A in AAF78102 (PubMed:10850993).Curated
Sequence conflicti258 – 2581A → G in AAF78102 (PubMed:10850993).Curated
Sequence conflicti306 – 3061H → Y in AAF78102 (PubMed:10850993).Curated
Sequence conflicti585 – 5851A → L in AAF78102 (PubMed:10850993).Curated
Sequence conflicti722 – 7232HD → QH in AAF78102 (PubMed:10850993).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126956 Genomic DNA. Translation: AAF78102.1.
AL939106 Genomic DNA. Translation: CAB57412.1.
RefSeqiNP_624873.1. NC_003888.3.
WP_011027206.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB57412; CAB57412; CAB57412.
GeneIDi1095983.
KEGGisco:SCO0560.
PATRICi23730638. VBIStrCoe124346_0541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126956 Genomic DNA. Translation: AAF78102.1.
AL939106 Genomic DNA. Translation: CAB57412.1.
RefSeqiNP_624873.1. NC_003888.3.
WP_011027206.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9RJH9.
SMRiQ9RJH9. Positions 33-740.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO0560.

Protein family/group databases

PeroxiBasei2351. ScoCP01_A3.

Proteomic databases

PRIDEiQ9RJH9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB57412; CAB57412; CAB57412.
GeneIDi1095983.
KEGGisco:SCO0560.
PATRICi23730638. VBIStrCoe124346_0541.

Phylogenomic databases

eggNOGiCOG0376. LUCA.
HOGENOMiHOG000218110.
InParanoidiQ9RJH9.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.
PhylomeDBiQ9RJH9.

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

« Hide 'large scale' publications
  1. "Regulation of the furA and catC operon, encoding a ferric uptake regulator homologue and catalase-peroxidase, respectively, in Streptomyces coelicolor A3(2)."
    Hahn J.-S., Oh S.-Y., Roe J.-H.
    J. Bacteriol. 182:3767-3774(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBUNIT.
    Strain: ATCC BAA-471 / A3(2) / M145.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiKATG_STRCO
AccessioniPrimary (citable) accession number: Q9RJH9
Secondary accession number(s): Q9KK92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 108 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.