katG encodes the bifunctional catalase-peroxidase (EC 1.11.1.21) of Pseudomonas putida KT2440, a soluble heme b-dependent hydroperoxidase. At a single heme active site it catalyzes two coupled reactions that detoxify hydrogen peroxide: a catalatic reaction dismutating H2O2 to water and oxygen (2 H2O2 -> O2 + 2 H2O), and a broad-spectrum peroxidatic reaction that reduces H2O2 to water using diverse organic electron donors (H2O2 + AH2 -> A + 2 H2O). The enzyme assembles as a homodimer or homotetramer and carries a covalent Trp-Tyr-Met crosslink that is required for the catalase but not the peroxidase activity. As a major H2O2-scavenging enzyme, KatG is a central component of the bacterial defense against oxidative stress.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0004096
catalase activity
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: Catalase activity is one of the two core molecular functions of this bifunctional enzyme. UniProt records the catalatic reaction (2 H2O2 = O2 + 2 H2O) under EC 1.11.1.21 and the FUNCTION line explicitly describes catalase activity.
Reason: The catalatic dismutation of hydrogen peroxide is a defining, well-supported core activity for a catalase-peroxidase and matches the UniProt catalytic-activity reaction and EC assignment.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Reaction=2 H2O2 = O2 + 2 H2O
file:PSEPK/katG/katG-uniprot.txt
Bifunctional enzyme with both catalase and broad-spectrum
file:PSEPK/katG/katG-uniprot.txt
PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE
|
|
GO:0004601
peroxidase activity
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: Peroxidase activity is the second core molecular function of this bifunctional enzyme. UniProt records the peroxidatic reaction (H2O2 + AH2 = A + 2 H2O) and describes broad-spectrum peroxidase activity.
Reason: The broad-spectrum peroxidatic reduction of H2O2 using organic electron donors is a defining core activity of catalase-peroxidases and is directly supported by the UniProt catalytic-activity reaction.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Reaction=H2O2 + AH2 = A + 2 H2O
file:PSEPK/katG/katG-uniprot.txt
Bifunctional enzyme with both catalase and broad-spectrum
|
|
GO:0005829
cytosol
|
IEA
GO_REF:0000118 |
KEEP AS NON CORE |
Summary: Cytosolic localization is a reasonable TreeGrafter prediction for a soluble bacterial catalase-peroxidase, but it is an IEA inference with no KT2440-specific localization evidence and is peripheral to the gene's core function.
Reason: Catalase-peroxidases are typically soluble cytoplasmic enzymes, so the prediction is biologically plausible, but the annotation is electronic only and the cellular location is not the core defining feature of the gene.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Homodimer or homotetramer.
|
|
GO:0006979
response to oxidative stress
|
IEA
GO_REF:0000002 |
ACCEPT |
Summary: Response to oxidative stress is a core biological process for KatG: by scavenging hydrogen peroxide it directly protects the cell against oxidative damage.
Reason: H2O2 decomposition by catalase-peroxidase is a principal mechanism of defense against oxidative stress, consistent with the bifunctional H2O2-detoxifying activity recorded in UniProt.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Bifunctional enzyme with both catalase and broad-spectrum
file:PSEPK/katG/katG-notes.md
central component of the cellular defense against oxidative/H2O2 stress.
|
|
GO:0020037
heme binding
|
IEA
GO_REF:0000120 |
MARK AS OVER ANNOTATED |
Summary: Heme b binding is mechanistically essential for this enzyme (UniProt records heme b as cofactor and an axial heme-iron binding residue), but as a cofactor-binding term it is broad relative to the specific catalase and peroxidase activity terms already present.
Reason: The annotation is correct and the heme is required for catalysis, but with the specific catalase and peroxidase molecular-function terms present, the generic heme-binding term adds little to the functional description and represents the cofactor-binding aspect rather than the core activity.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Name=heme b; Xref=ChEBI:CHEBI:60344
file:PSEPK/katG/katG-uniprot.txt
Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
|
|
GO:0042744
hydrogen peroxide catabolic process
|
IEA
GO_REF:0000118 |
ACCEPT |
Summary: Hydrogen peroxide catabolic process is the core biological process directly effected by both the catalase and peroxidase activities of KatG, which consume H2O2.
Reason: Both UniProt catalytic-activity reactions consume hydrogen peroxide, making H2O2 catabolism the most direct process-level description of this enzyme's role.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Reaction=2 H2O2 = O2 + 2 H2O
file:PSEPK/katG/katG-uniprot.txt
Reaction=H2O2 + AH2 = A + 2 H2O
|
|
GO:0070301
cellular response to hydrogen peroxide
|
IEA
GO_REF:0000118 |
KEEP AS NON CORE |
Summary: Cellular response to hydrogen peroxide is consistent with KatG's role in decomposing H2O2 as part of the cell's defensive reaction to peroxide exposure; it is a valid but somewhat more peripheral process term than the direct H2O2 catabolic process.
Reason: The annotation is biologically reasonable for an H2O2-scavenging enzyme, but the direct H2O2 catabolic process term more precisely captures the enzyme's core contribution; this response term is retained as non-core.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Bifunctional enzyme with both catalase and broad-spectrum
|
|
GO:0098869
cellular oxidant detoxification
|
IEA
GO_REF:0000120 |
KEEP AS NON CORE |
Summary: Cellular oxidant detoxification is correctly inferred from the catalase and peroxidase activities (the GOA entry derives it from GO:0004096 and GO:0004601), capturing the protective antioxidant role of KatG.
Reason: The term accurately describes the detoxification outcome of H2O2 decomposition but is more general than the specific hydrogen peroxide catabolic process term; it is retained as a valid non-core process annotation.
Supporting Evidence:
file:PSEPK/katG/katG-uniprot.txt
Bifunctional enzyme with both catalase and broad-spectrum
file:PSEPK/katG/katG-notes.md
central component of the cellular defense against oxidative/H2O2 stress.
|
Q: Is katG expression in Pseudomonas putida KT2440 induced by hydrogen peroxide or governed by an OxyR-type regulator, and how does it partition with other catalases in H2O2 defense?
Suggested experts: Bacterial oxidative-stress regulation specialists, Pseudomonas physiologists
Q: What is the relative in vivo contribution of the catalatic versus peroxidatic activity of KatG to H2O2 detoxification under different growth and stress conditions?
Suggested experts: Enzyme mechanism researchers, Redox biochemists
Experiment: Delete katG (PP_3668) in KT2440, optionally in combination with other catalase genes, and measure H2O2 sensitivity, residual catalase/peroxidase activity, and survival under oxidative stress.
Type: Gene knockout and phenotyping
Experiment: Purify recombinant KatG and confirm heme b incorporation, catalase and peroxidase activities, and the dependence of catalatic (but not peroxidatic) activity on the Trp-Tyr-Met crosslink via site-directed mutagenesis.
Type: Enzyme assay and cofactor analysis
Experiment: Fractionate KT2440 to verify the predicted cytosolic localization of KatG and rule out periplasmic or membrane association.
Type: Subcellular fractionation
UniProt: Q88GQ0 (KATG_PSEPK), locus PP_3668, 751 aa, EC 1.11.1.21.
KatG is a bifunctional, heme b-dependent catalase-peroxidase (hydroperoxidase, HPI-type).
It decomposes hydrogen peroxide by two coupled activities at a single heme active site:
a catalatic reaction (2 H2O2 -> O2 + 2 H2O) and a broad-spectrum peroxidatic reaction
(H2O2 + AH2 -> A + 2 H2O), oxidizing diverse electron-donor substrates. These activities
make KatG a central component of the cellular defense against oxidative/H2O2 stress.
Core molecular functions: catalase activity (GO:0004096) and peroxidase activity
(GO:0004601) — both directly supported by the two UniProt catalytic-activity reactions
and the bifunctional FUNCTION statement.
Core biological processes: response to oxidative stress (GO:0006979), hydrogen peroxide
catabolic process (GO:0042744), cellular response to hydrogen peroxide (GO:0070301),
and cellular oxidant detoxification (GO:0098869) — all consistent with H2O2-decomposing
function. These are accepted; the cellular-response/detoxification terms are reasonable
but more peripheral than the direct catabolic process.
Broad terms relative to specific function: heme binding (GO:0020037) and metal ion
binding (the keyword-derived GO:0046872, not separately listed in the GOA TSV but
present in the UniProt cross-references) describe cofactor binding rather than the
catalytic function. Heme binding is a real, mechanistically essential property
(supported by the COFACTOR and axial-binding-residue evidence) and is informative for a
heme enzyme, so it is retained but flagged as non-core/over-annotated relative to the
specific catalase and peroxidase activity terms. "metal ion binding" is the broadest
of these and over-annotated when heme binding is present.
Cellular component: cytosol (GO:0005829) is a reasonable TreeGrafter prediction for a
soluble bacterial catalase-peroxidase; retained as non-core (IEA, no direct localization
evidence for KT2440).
Caveat: evidence for this entry is "Inferred from homology" (PE 3) and all GO
annotations are IEA. No KT2440-specific experimental publication characterizing KatG was
available; the only cited reference (PMID:12534463) is the genome sequencing paper.
id: Q88GQ0
gene_symbol: katG
product_type: PROTEIN
aliases:
- PP_3668
status: COMPLETE
taxon:
id: NCBITaxon:160488
label: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
/ KT2440)
description: >-
katG encodes the bifunctional catalase-peroxidase (EC 1.11.1.21) of Pseudomonas
putida KT2440, a soluble heme b-dependent hydroperoxidase. At a single heme active
site it catalyzes two coupled reactions that detoxify hydrogen peroxide: a catalatic
reaction dismutating H2O2 to water and oxygen (2 H2O2 -> O2 + 2 H2O), and a
broad-spectrum peroxidatic reaction that reduces H2O2 to water using diverse organic
electron donors (H2O2 + AH2 -> A + 2 H2O). The enzyme assembles as a homodimer or
homotetramer and carries a covalent Trp-Tyr-Met crosslink that is required for the
catalase but not the peroxidase activity. As a major H2O2-scavenging enzyme, KatG is
a central component of the bacterial defense against oxidative stress.
existing_annotations:
- term:
id: GO:0004096
label: catalase activity
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: enables
review:
summary: >-
Catalase activity is one of the two core molecular functions of this bifunctional
enzyme. UniProt records the catalatic reaction (2 H2O2 = O2 + 2 H2O) under EC
1.11.1.21 and the FUNCTION line explicitly describes catalase activity.
action: ACCEPT
reason: >-
The catalatic dismutation of hydrogen peroxide is a defining, well-supported core
activity for a catalase-peroxidase and matches the UniProt catalytic-activity
reaction and EC assignment.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Reaction=2 H2O2 = O2 + 2 H2O"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"
- term:
id: GO:0004601
label: peroxidase activity
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: enables
review:
summary: >-
Peroxidase activity is the second core molecular function of this bifunctional
enzyme. UniProt records the peroxidatic reaction (H2O2 + AH2 = A + 2 H2O) and
describes broad-spectrum peroxidase activity.
action: ACCEPT
reason: >-
The broad-spectrum peroxidatic reduction of H2O2 using organic electron donors is
a defining core activity of catalase-peroxidases and is directly supported by the
UniProt catalytic-activity reaction.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Reaction=H2O2 + AH2 = A + 2 H2O"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- term:
id: GO:0005829
label: cytosol
evidence_type: IEA
original_reference_id: GO_REF:0000118
qualifier: located_in
review:
summary: >-
Cytosolic localization is a reasonable TreeGrafter prediction for a soluble
bacterial catalase-peroxidase, but it is an IEA inference with no KT2440-specific
localization evidence and is peripheral to the gene's core function.
action: KEEP_AS_NON_CORE
reason: >-
Catalase-peroxidases are typically soluble cytoplasmic enzymes, so the prediction
is biologically plausible, but the annotation is electronic only and the cellular
location is not the core defining feature of the gene.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Homodimer or homotetramer."
- term:
id: GO:0006979
label: response to oxidative stress
evidence_type: IEA
original_reference_id: GO_REF:0000002
qualifier: involved_in
review:
summary: >-
Response to oxidative stress is a core biological process for KatG: by scavenging
hydrogen peroxide it directly protects the cell against oxidative damage.
action: ACCEPT
reason: >-
H2O2 decomposition by catalase-peroxidase is a principal mechanism of defense
against oxidative stress, consistent with the bifunctional H2O2-detoxifying
activity recorded in UniProt.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- reference_id: file:PSEPK/katG/katG-notes.md
supporting_text: >-
central component of the cellular defense against oxidative/H2O2 stress.
- term:
id: GO:0020037
label: heme binding
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: enables
review:
summary: >-
Heme b binding is mechanistically essential for this enzyme (UniProt records heme
b as cofactor and an axial heme-iron binding residue), but as a cofactor-binding
term it is broad relative to the specific catalase and peroxidase activity terms
already present.
action: MARK_AS_OVER_ANNOTATED
reason: >-
The annotation is correct and the heme is required for catalysis, but with the
specific catalase and peroxidase molecular-function terms present, the generic
heme-binding term adds little to the functional description and represents the
cofactor-binding aspect rather than the core activity.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Name=heme b; Xref=ChEBI:CHEBI:60344"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."
- term:
id: GO:0042744
label: hydrogen peroxide catabolic process
evidence_type: IEA
original_reference_id: GO_REF:0000118
qualifier: involved_in
review:
summary: >-
Hydrogen peroxide catabolic process is the core biological process directly
effected by both the catalase and peroxidase activities of KatG, which consume
H2O2.
action: ACCEPT
reason: >-
Both UniProt catalytic-activity reactions consume hydrogen peroxide, making H2O2
catabolism the most direct process-level description of this enzyme's role.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Reaction=2 H2O2 = O2 + 2 H2O"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Reaction=H2O2 + AH2 = A + 2 H2O"
- term:
id: GO:0070301
label: cellular response to hydrogen peroxide
evidence_type: IEA
original_reference_id: GO_REF:0000118
qualifier: involved_in
review:
summary: >-
Cellular response to hydrogen peroxide is consistent with KatG's role in
decomposing H2O2 as part of the cell's defensive reaction to peroxide exposure;
it is a valid but somewhat more peripheral process term than the direct H2O2
catabolic process.
action: KEEP_AS_NON_CORE
reason: >-
The annotation is biologically reasonable for an H2O2-scavenging enzyme, but the
direct H2O2 catabolic process term more precisely captures the enzyme's core
contribution; this response term is retained as non-core.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- term:
id: GO:0098869
label: cellular oxidant detoxification
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: involved_in
review:
summary: >-
Cellular oxidant detoxification is correctly inferred from the catalase and
peroxidase activities (the GOA entry derives it from GO:0004096 and GO:0004601),
capturing the protective antioxidant role of KatG.
action: KEEP_AS_NON_CORE
reason: >-
The term accurately describes the detoxification outcome of H2O2 decomposition but
is more general than the specific hydrogen peroxide catabolic process term; it is
retained as a valid non-core process annotation.
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- reference_id: file:PSEPK/katG/katG-notes.md
supporting_text: >-
central component of the cellular defense against oxidative/H2O2 stress.
references:
- id: GO_REF:0000002
title: Gene Ontology annotation through association of InterPro records with GO terms
findings: []
- id: GO_REF:0000118
title: TreeGrafter-generated GO annotations
findings: []
- id: GO_REF:0000120
title: Combined Automated Annotation using Multiple IEA Methods
findings: []
- id: file:PSEPK/katG/katG-uniprot.txt
title: UniProtKB Q88GQ0 KATG_PSEPK Pseudomonas putida KT2440
findings:
- statement: >-
UniProt describes KatG as a bifunctional enzyme with both catalase and
broad-spectrum peroxidase activity.
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- statement: >-
UniProt records the catalatic reaction dismutating hydrogen peroxide to oxygen and
water.
supporting_text: "Reaction=2 H2O2 = O2 + 2 H2O"
- statement: >-
UniProt records the peroxidatic reaction reducing hydrogen peroxide using an
organic electron donor.
supporting_text: "Reaction=H2O2 + AH2 = A + 2 H2O"
- statement: >-
UniProt records heme b as the cofactor, with one heme b bound per dimer.
supporting_text: "Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."
- statement: >-
UniProt notes the Trp-Tyr-Met crosslink is required for the catalase but not the
peroxidase activity.
supporting_text: "for the catalase, but not the peroxidase activity of the enzyme."
- id: file:interpro/panther/PTHR30555/PTHR30555-metadata.yaml
title: >-
PANTHER family PTHR30555 (HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE),
subfamily PTHR30555:SF0 (CATALASE-PEROXIDASE)
findings:
- statement: >-
katG (Q88GQ0) is classified in PANTHER family PTHR30555 and subfamily
PTHR30555:SF0.
- statement: >-
The PANTHER family and subfamily names confirm the bifunctional
catalase-peroxidase function of KatG.
- id: PMID:12534463
title: >-
Complete genome sequence and comparative analysis of the metabolically versatile
Pseudomonas putida KT2440
findings:
- statement: >-
The KT2440 genome sequencing and annotation effort that established the PP_3668
(katG) locus and reference proteome entry.
full_text_unavailable: true
- id: file:PSEPK/katG/katG-notes.md
title: Curator notes for katG in Pseudomonas putida KT2440
findings:
- statement: >-
Synthesis of UniProt evidence describing KatG as a central H2O2-scavenging enzyme
in oxidative stress defense.
supporting_text: >-
central component of the cellular defense against oxidative/H2O2 stress.
core_functions:
- description: >-
Heme b-dependent catalatic decomposition of hydrogen peroxide, dismutating two
molecules of H2O2 into oxygen and water as a primary H2O2-detoxifying activity.
molecular_function:
id: GO:0004096
label: catalase activity
directly_involved_in:
- id: GO:0042744
label: hydrogen peroxide catabolic process
- id: GO:0006979
label: response to oxidative stress
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Reaction=2 H2O2 = O2 + 2 H2O"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
- description: >-
Heme b-dependent broad-spectrum peroxidatic reduction of hydrogen peroxide using
diverse organic electron donors, contributing to oxidative-stress defense.
molecular_function:
id: GO:0004601
label: peroxidase activity
directly_involved_in:
- id: GO:0042744
label: hydrogen peroxide catabolic process
- id: GO:0006979
label: response to oxidative stress
supported_by:
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Reaction=H2O2 + AH2 = A + 2 H2O"
- reference_id: file:PSEPK/katG/katG-uniprot.txt
supporting_text: "Bifunctional enzyme with both catalase and broad-spectrum"
proposed_new_terms: []
suggested_questions:
- question: >-
Is katG expression in Pseudomonas putida KT2440 induced by hydrogen peroxide or
governed by an OxyR-type regulator, and how does it partition with other catalases
in H2O2 defense?
experts:
- Bacterial oxidative-stress regulation specialists
- Pseudomonas physiologists
- question: >-
What is the relative in vivo contribution of the catalatic versus peroxidatic
activity of KatG to H2O2 detoxification under different growth and stress
conditions?
experts:
- Enzyme mechanism researchers
- Redox biochemists
suggested_experiments:
- experiment_type: Gene knockout and phenotyping
description: >-
Delete katG (PP_3668) in KT2440, optionally in combination with other catalase
genes, and measure H2O2 sensitivity, residual catalase/peroxidase activity, and
survival under oxidative stress.
- experiment_type: Enzyme assay and cofactor analysis
description: >-
Purify recombinant KatG and confirm heme b incorporation, catalase and peroxidase
activities, and the dependence of catalatic (but not peroxidatic) activity on the
Trp-Tyr-Met crosslink via site-directed mutagenesis.
- experiment_type: Subcellular fractionation
description: >-
Fractionate KT2440 to verify the predicted cytosolic localization of KatG and rule
out periplasmic or membrane association.