btuE

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0034599 cellular response to oxidative stress	IBA GO_REF:0000033	ACCEPT	Summary: Cellular response to oxidative stress, propagated from the PANTHER PTHR11592 root node PTN002480721. Q8P365 descends from that node through the gammaproteobacterial BtuE node PTN000173904. Reason: This IBA follows from the PAINT IBD at the family root PTN002480721, and the PANTHER 19 tree places Q8P365 beneath it with no intervening IRD/NOT on its lineage. The PAINT negations of this family are on eutherian and fungal nodes only. In the closest characterized member of the same subfamily and PAINT clade, E. coli BtuE (P06610), btuE is induced by oxidative-stress elicitors, and the purified enzyme reduces H2O2 and organic hydroperoxides. A peroxide-scavenging enzyme whose expression responds to oxidants does part of the work of the cellular response to oxidative stress. No Xanthomonas-specific experiment exists, but the phylogenetic inference is sound. Supporting Evidence: PMID:20621065 The btuE gene was induced when cells were exposed to oxidative stress elicitors that included potassium tellurite, menadione and hydrogen peroxide, among others, suggesting that BtuE could participate in the E. coli response to reactive oxygen species. file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md Q8P365 descends from PTN000173904 (Gammaproteobacteria, subfamily PTHR11592:SF40), the same node that contains experimentally characterized E. coli BtuE (P06610).
GO:0004601 peroxidase activity	IEA GO_REF:0000002	MODIFY	Summary: Peroxidase activity from the InterPro IPR000889 mapping is correct but general. Clade evidence supports the more specific thioredoxin-dependent peroxiredoxin activity, with glutathione peroxidase activity as a secondary activity. Reason: Q8P365 conserves the full GPx catalytic tetrad (C37, Q71, W143, N144), plus the resolving-cysteine position C83, which aligns to E. coli BtuE C83. Both proteins descend from PAINT node PTN000173904 in subfamily PTHR11592:SF40, where PAINT curators placed GO:0008379 thioredoxin peroxidase activity by IBD from P06610. Purified E. coli BtuE uses thioredoxins A or C in preference to glutathione for H2O2, cumene, tert-butyl and linoleic acid hydroperoxides. GO:0140824 thioredoxin-dependent peroxiredoxin activity (a hydroperoxide-general parent of GO:0008379) is the best replacement, because substrate breadth was shown. GO:0004602 glutathione peroxidase activity is also listed. It is placed by PAINT at the family root, and E. coli BtuE shows glutathione-dependent H2O2 decomposition in vitro. The earlier version of this review proposed GO:0004602 alone, which ignored the thioredoxin preference of the clade. Both proposed terms are is_a descendants of GO:0004601. Proposed replacements: thioredoxin-dependent peroxiredoxin activity glutathione peroxidase activity Supporting Evidence: PMID:20621065 Figure 2 shows that BtuE uses preferentially thioredoxins A or C as reducing agents irrespective of the peroxide substrate. PMID:20621065 Purified BtuE decomposes in vitro hydrogen peroxide in a glutathione-dependent manner. file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md Q8P365 C37 aligns to P06610 C37 (peroxidatic cysteine), and Q8P365 C83 aligns to P06610 C83 (resolving-cysteine position on helix alpha2 of atypical 2-Cys GPx-like peroxiredoxins). file:XANCP/Q8P365/Q8P365-uniprot.txt Belongs to the glutathione peroxidase family.
GO:0006979 response to oxidative stress	IEA GO_REF:0000002	TOO GENERAL	Summary: Response to oxidative stress is true for Q8P365, but it is an ancestor of cellular response to oxidative stress (GO:0034599), which is accepted in this review. Reason: The claim is correct for a BtuE-clade peroxidase, as the IBA row above sets out. GO:0034599 already entails it, so the broader InterPro2GO term adds no information. The judgment concerns the term only: the claim is not false. Supporting Evidence: PMID:20621065 suggesting that BtuE could participate in the E. coli response to reactive oxygen species
GO:0098869 cellular oxidant detoxification	IEA GO_REF:0000108	ACCEPT	Summary: Cellular oxidant detoxification, inferred logically from peroxidase activity. This is the process in which a cytoplasmic thiol peroxidase directly takes part. Reason: The enzyme itself performs the detoxifying step: reduction of H2O2 and organic hydroperoxides to water or alcohols. That matches GO:0098869, which GO places as a part_of parent of the peroxidase and peroxiredoxin activities. The activity is supported for the BtuE clade by PAINT node placement and by E. coli BtuE biochemistry, and the catalytic residues are conserved in Q8P365. Supporting Evidence: PMID:20621065 BtuE also utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, confirming that its active site confers non-specific peroxidase activity. file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md Transfer of BtuE's thioredoxin-dependent hydroperoxide reductase activity is supported by node placement and by conservation of both the peroxidatic and resolving cysteines.

GO Term

Evidence

Action

Reason

GO:0034599 cellular response to oxidative stress

IBA
GO_REF:0000033

Summary: Cellular response to oxidative stress, propagated from the PANTHER PTHR11592 root node PTN002480721. Q8P365 descends from that node through the gammaproteobacterial BtuE node PTN000173904.

Reason: This IBA follows from the PAINT IBD at the family root PTN002480721, and the PANTHER 19 tree places Q8P365 beneath it with no intervening IRD/NOT on its lineage. The PAINT negations of this family are on eutherian and fungal nodes only. In the closest characterized member of the same subfamily and PAINT clade, E. coli BtuE (P06610), btuE is induced by oxidative-stress elicitors, and the purified enzyme reduces H2O2 and organic hydroperoxides. A peroxide-scavenging enzyme whose expression responds to oxidants does part of the work of the cellular response to oxidative stress. No Xanthomonas-specific experiment exists, but the phylogenetic inference is sound.

Supporting Evidence:

PMID:20621065

The btuE gene was induced when cells were exposed to oxidative stress elicitors that included potassium tellurite, menadione and hydrogen peroxide, among others, suggesting that BtuE could participate in the E. coli response to reactive oxygen species.

file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md

Q8P365 descends from PTN000173904 (Gammaproteobacteria, subfamily PTHR11592:SF40), the same node that contains experimentally characterized E. coli BtuE (P06610).

GO:0004601 peroxidase activity

IEA
GO_REF:0000002

MODIFY

Summary: Peroxidase activity from the InterPro IPR000889 mapping is correct but general. Clade evidence supports the more specific thioredoxin-dependent peroxiredoxin activity, with glutathione peroxidase activity as a secondary activity.

Reason: Q8P365 conserves the full GPx catalytic tetrad (C37, Q71, W143, N144), plus the resolving-cysteine position C83, which aligns to E. coli BtuE C83. Both proteins descend from PAINT node PTN000173904 in subfamily PTHR11592:SF40, where PAINT curators placed GO:0008379 thioredoxin peroxidase activity by IBD from P06610. Purified E. coli BtuE uses thioredoxins A or C in preference to glutathione for H2O2, cumene, tert-butyl and linoleic acid hydroperoxides. GO:0140824 thioredoxin-dependent peroxiredoxin activity (a hydroperoxide-general parent of GO:0008379) is the best replacement, because substrate breadth was shown. GO:0004602 glutathione peroxidase activity is also listed. It is placed by PAINT at the family root, and E. coli BtuE shows glutathione-dependent H2O2 decomposition in vitro. The earlier version of this review proposed GO:0004602 alone, which ignored the thioredoxin preference of the clade. Both proposed terms are is_a descendants of GO:0004601.

Proposed replacements: thioredoxin-dependent peroxiredoxin activity glutathione peroxidase activity

Supporting Evidence:

PMID:20621065

Figure 2 shows that BtuE uses preferentially thioredoxins A or C as reducing agents irrespective of the peroxide substrate.

PMID:20621065

Purified BtuE decomposes in vitro hydrogen peroxide in a glutathione-dependent manner.

file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md

Q8P365 C37 aligns to P06610 C37 (peroxidatic cysteine), and Q8P365 C83 aligns to P06610 C83 (resolving-cysteine position on helix alpha2 of atypical 2-Cys GPx-like peroxiredoxins).

file:XANCP/Q8P365/Q8P365-uniprot.txt

Belongs to the glutathione peroxidase family.

GO:0006979 response to oxidative stress

IEA
GO_REF:0000002

TOO GENERAL

Summary: Response to oxidative stress is true for Q8P365, but it is an ancestor of cellular response to oxidative stress (GO:0034599), which is accepted in this review.

Reason: The claim is correct for a BtuE-clade peroxidase, as the IBA row above sets out. GO:0034599 already entails it, so the broader InterPro2GO term adds no information. The judgment concerns the term only: the claim is not false.

Supporting Evidence:

PMID:20621065

suggesting that BtuE could participate in the E. coli response to reactive oxygen species

GO:0098869 cellular oxidant detoxification

IEA
GO_REF:0000108

Summary: Cellular oxidant detoxification, inferred logically from peroxidase activity. This is the process in which a cytoplasmic thiol peroxidase directly takes part.

Reason: The enzyme itself performs the detoxifying step: reduction of H2O2 and organic hydroperoxides to water or alcohols. That matches GO:0098869, which GO places as a part_of parent of the peroxidase and peroxiredoxin activities. The activity is supported for the BtuE clade by PAINT node placement and by E. coli BtuE biochemistry, and the catalytic residues are conserved in Q8P365.

Supporting Evidence:

PMID:20621065

BtuE also utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, confirming that its active site confers non-specific peroxidase activity.

file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md

Transfer of BtuE's thioredoxin-dependent hydroperoxide reductase activity is supported by node placement and by conservation of both the peroxidatic and resolving cysteines.

Core Functions

Cytoplasmic thiol peroxidase of the BtuE clade. It reduces hydrogen peroxide and organic or lipid hydroperoxides through a peroxidatic cysteine (Cys37), with a conserved resolving cysteine (Cys83). Thioredoxin is predicted to be the preferred reductant, as for E. coli BtuE.

Molecular Function:

thioredoxin-dependent peroxiredoxin activity

Directly Involved In:

cellular oxidant detoxification cellular response to oxidative stress

Supporting Evidence:

PMID:20621065
Figure 2 shows that BtuE uses preferentially thioredoxins A or C as reducing agents irrespective of the peroxide substrate.
file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md
Q8P365 descends from PTN000173904 (Gammaproteobacteria, subfamily PTHR11592:SF40), the same node that contains experimentally characterized E. coli BtuE (P06610).

External Prediction Reviews

These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.

ProtNLM2 External predictions

View prediction review YAML · Q8P365-protnlm-predictions-review.yaml · Review status: COMPLETE

Q8P365 is a BtuE-subfamily glutathione peroxidase-fold thiol peroxidase. By phylogenetic transfer from E. coli BtuE it takes part in the cellular response to oxidative stress. The single ProtNLM2 prediction, response to oxidative stress, is correct but broader than the accepted cellular-response annotation.

Source documents: genes/XANCP/Q8P365/Q8P365-uniprot.txt · genes/XANCP/Q8P365/Q8P365-goa.tsv · genes/XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md · publications/PMID_20621065.md

Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.

GO:0006979 response to oxidative stress GO_BP

LSP — Less precise than existing annotation Review score: 2/2

Prediction method: ProtNLM2 · Version: UniProt 2024_06 pilot

Review rationale: Q8P365 belongs to the glutathione peroxidase family and the BtuE subfamily (PANTHER PTHR11592:SF40), and descends from the gammaproteobacterial PAINT node PTN000173904 that contains experimentally characterized E. coli BtuE (P06610). It conserves the peroxidatic Cys37 active site. Purified E. coli BtuE decomposes peroxides and btuE is induced by oxidative-stress elicitors (PMID:20621065), which supports transfer of a protective role in the oxidative-stress response. The gene already carries an accepted IBA for GO:0034599 cellular response to oxidative stress, an is_a descendant of the predicted GO:0006979 (OLS4 ancestry), and the gene review marks the GOA IEA row for GO:0006979 itself as TOO_GENERAL. The prediction is correct but less precise than the existing supported annotation. No experiment on the Xanthomonas protein itself was found in a PubMed search.

Supporting Evidence:

file:XANCP/Q8P365/Q8P365-uniprot.txt: "Belongs to the glutathione peroxidase family."
file:XANCP/Q8P365/Q8P365-uniprot.txt: "PTHR11592:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE"
file:XANCP/Q8P365/Q8P365-bioinformatics/RESULTS-rereview.md: "Q8P365 descends from PTN000173904 (Gammaproteobacteria, subfamily PTHR11592:SF40), the same node that contains experimentally characterized E. coli BtuE (P06610)."
PMID:20621065: "Purified BtuE decomposes in vitro hydrogen peroxide in a glutathione-dependent manner"
PMID:20621065: "The btuE gene was induced when cells were exposed to oxidative stress elicitors that included potassium tellurite, menadione and hydrogen peroxide"

Gene Description

Existing Annotations Review

Core Functions

Cytoplasmic thiol peroxidase of the BtuE clade. It reduces hydrogen peroxide and organic or lipid hydroperoxides through a peroxidatic cysteine (Cys37), with a conserved resolving cysteine (Cys83). Thioredoxin is predicted to be the preferred reductant, as for E. coli BtuE.

References

Suggested Questions for Experts

Suggested Experiments

External Prediction Reviews

ProtNLM2 External predictions

Deep Research

Falcon

📚 Additional Documentation

Notes

📄 View Raw YAML