Q53353 (LSD-I) is lignostilbene-alpha,beta-dioxygenase isozyme I of Sphingomonas (Pseudomonas) paucimobilis TMY1009, one of the founding members of the stilbene cleavage oxygenase (SCO) / carotenoid cleavage oxygenase (CCO) superfamily and a companion isozyme to LSD-III (lsdB). It is a non-heme iron dioxygenase that cleaves the interphenyl (Calpha-Cbeta) double bond of lignostilbene (1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene) with molecular oxygen to yield two molecules of vanillin (EC 1.13.11.43), acting in the catabolism of lignin-derived stilbenes. Despite automated annotations to the contrary, LSD-I is not a carotenoid cleavage enzyme.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0010436
carotenoid dioxygenase activity
|
IEA
GO_REF:0000118 |
REMOVE |
Summary: Automated (IEA / TreeGrafter) carotenoid dioxygenase activity - wrong substrate class and directly contradicted by this gene's own experimental annotation to lignostilbene alpha,beta-dioxygenase activity (GO:0050054, IDA). A TreeGrafter over-propagation from the mixed CCO family.
Reason: LSD-I is an experimentally characterized lignostilbene dioxygenase (EC 1.13.11.43), not a carotenoid enzyme; the correct specific MF (GO:0050054) is already present by IDA. Same substrate-class error as LSD-III, NOV1/NOV2, Rco1, and cao-1.
|
|
GO:0016121
carotene catabolic process
|
IEA
GO_REF:0000118 |
REMOVE |
Summary: Automated (IEA / TreeGrafter) carotene catabolic process. Wrong substrate class; LSD-I's real process is lignin/stilbene catabolism, already captured experimentally (GO:0046274, IDA).
Reason: Contradicted by the gene's own IDA lignin catabolic process annotation; TreeGrafter over-propagation.
|
|
GO:0016702
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
|
IEA
GO_REF:0000002 |
ACCEPT |
Summary: InterPro-based (IEA) dioxygenase MF term; correct general parent of the specific lignostilbene activity.
Reason: Accurate general dioxygenase MF.
|
|
GO:0050054
lignostilbene alpha beta-dioxygenase activity
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: Automated (IEA) annotation of the specific lignostilbene alpha,beta-dioxygenase activity, also supported by IDA. The correct, specific MF term for LSD-I.
Reason: Core molecular function, corroborated by IDA.
|
|
GO:0046274
lignin catabolic process
|
IDA
PMID:7763880 Structural and enzymatical comparison of lignostilbene-alpha... |
ACCEPT |
Summary: Direct experimental (IDA) annotation of lignin catabolic process; LSD cleaves lignin-derived stilbene (lignostilbene) to vanillin.
Reason: Core biological process, experimentally supported; the correct (non-carotenoid) process.
Supporting Evidence:
PMID:7763880
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas
|
|
GO:0050054
lignostilbene alpha beta-dioxygenase activity
|
IDA
PMID:7763880 Structural and enzymatical comparison of lignostilbene-alpha... |
ACCEPT |
Summary: Direct experimental (IDA) annotation of lignostilbene alpha,beta-dioxygenase activity from the purification/characterization of the LSD isozymes. Core, correct molecular function of LSD-I.
Reason: Core catalytic function (EC 1.13.11.43), directly demonstrated. The specific term the TreeGrafter carotenoid annotations should never have overridden.
Supporting Evidence:
PMID:7763880
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas
|
|
GO:0005506
iron ion binding
|
IDA
DOI:10.1271/bbb1961.53.2757 |
ACCEPT |
Summary: Direct experimental (IDA) annotation of iron binding from the original LSD-I purification. LSD/SCO enzymes use a non-heme mononuclear iron center.
Reason: Bona fide cofactor of this non-heme iron dioxygenase, experimentally supported.
|
|
GO:0046274
lignin catabolic process
|
IDA
DOI:10.1271/bbb1961.53.2757 |
ACCEPT |
Summary: Direct experimental (IDA) annotation of lignin catabolic process from the original LSD-I characterization.
Reason: Core biological process, experimentally supported (duplicate term from a distinct reference).
|
|
GO:0050054
lignostilbene alpha beta-dioxygenase activity
|
IDA
DOI:10.1271/bbb1961.53.2757 |
ACCEPT |
Summary: Direct experimental (IDA) annotation of lignostilbene alpha,beta-dioxygenase activity from the original LSD-I purification and characterization.
Reason: Core catalytic function, experimentally supported (the founding LSD-I characterization).
|
Q: Like LSD-III, LSD-I carries the correct specific IDA annotations yet also the contradictory TreeGrafter carotenoid terms; should these be removed and the TreeGrafter rule corrected for the SCO branch of the CCO family?
id: Q53353
gene_symbol: Q53353
product_type: PROTEIN
status: IN_PROGRESS
taxon:
id: NCBITaxon:13689
label: Sphingomonas paucimobilis
description: >-
Q53353 (LSD-I) is lignostilbene-alpha,beta-dioxygenase isozyme I of Sphingomonas (Pseudomonas)
paucimobilis TMY1009, one of the founding members of the stilbene cleavage oxygenase (SCO) /
carotenoid cleavage oxygenase (CCO) superfamily and a companion isozyme to LSD-III (lsdB). It is a
non-heme iron dioxygenase that cleaves the interphenyl (Calpha-Cbeta) double bond of lignostilbene
(1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene) with molecular oxygen to yield two molecules of vanillin
(EC 1.13.11.43), acting in the catabolism of lignin-derived stilbenes. Despite automated annotations
to the contrary, LSD-I is not a carotenoid cleavage enzyme.
existing_annotations:
- term:
id: GO:0010436
label: carotenoid dioxygenase activity
evidence_type: IEA
original_reference_id: GO_REF:0000118
qualifier: enables
review:
summary: >-
Automated (IEA / TreeGrafter) carotenoid dioxygenase activity - wrong substrate class and directly
contradicted by this gene's own experimental annotation to lignostilbene alpha,beta-dioxygenase
activity (GO:0050054, IDA). A TreeGrafter over-propagation from the mixed CCO family.
action: REMOVE
reason: >-
LSD-I is an experimentally characterized lignostilbene dioxygenase (EC 1.13.11.43), not a
carotenoid enzyme; the correct specific MF (GO:0050054) is already present by IDA. Same
substrate-class error as LSD-III, NOV1/NOV2, Rco1, and cao-1.
- term:
id: GO:0016121
label: carotene catabolic process
evidence_type: IEA
original_reference_id: GO_REF:0000118
qualifier: involved_in
review:
summary: >-
Automated (IEA / TreeGrafter) carotene catabolic process. Wrong substrate class; LSD-I's real
process is lignin/stilbene catabolism, already captured experimentally (GO:0046274, IDA).
action: REMOVE
reason: >-
Contradicted by the gene's own IDA lignin catabolic process annotation; TreeGrafter
over-propagation.
- term:
id: GO:0016702
label: oxidoreductase activity, acting on single donors with incorporation of
molecular oxygen, incorporation of two atoms of oxygen
evidence_type: IEA
original_reference_id: GO_REF:0000002
qualifier: enables
review:
summary: >-
InterPro-based (IEA) dioxygenase MF term; correct general parent of the specific lignostilbene
activity.
action: ACCEPT
reason: >-
Accurate general dioxygenase MF.
- term:
id: GO:0050054
label: lignostilbene alpha beta-dioxygenase activity
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: enables
review:
summary: >-
Automated (IEA) annotation of the specific lignostilbene alpha,beta-dioxygenase activity, also
supported by IDA. The correct, specific MF term for LSD-I.
action: ACCEPT
reason: >-
Core molecular function, corroborated by IDA.
- term:
id: GO:0046274
label: lignin catabolic process
evidence_type: IDA
original_reference_id: PMID:7763880
qualifier: involved_in
review:
summary: >-
Direct experimental (IDA) annotation of lignin catabolic process; LSD cleaves lignin-derived
stilbene (lignostilbene) to vanillin.
action: ACCEPT
reason: >-
Core biological process, experimentally supported; the correct (non-carotenoid) process.
supported_by:
- reference_id: PMID:7763880
supporting_text: >-
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas
- term:
id: GO:0050054
label: lignostilbene alpha beta-dioxygenase activity
evidence_type: IDA
original_reference_id: PMID:7763880
qualifier: enables
review:
summary: >-
Direct experimental (IDA) annotation of lignostilbene alpha,beta-dioxygenase activity from the
purification/characterization of the LSD isozymes. Core, correct molecular function of LSD-I.
action: ACCEPT
reason: >-
Core catalytic function (EC 1.13.11.43), directly demonstrated. The specific term the TreeGrafter
carotenoid annotations should never have overridden.
supported_by:
- reference_id: PMID:7763880
supporting_text: >-
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas
- term:
id: GO:0005506
label: iron ion binding
evidence_type: IDA
original_reference_id: DOI:10.1271/bbb1961.53.2757
qualifier: enables
review:
summary: >-
Direct experimental (IDA) annotation of iron binding from the original LSD-I purification. LSD/SCO
enzymes use a non-heme mononuclear iron center.
action: ACCEPT
reason: >-
Bona fide cofactor of this non-heme iron dioxygenase, experimentally supported.
- term:
id: GO:0046274
label: lignin catabolic process
evidence_type: IDA
original_reference_id: DOI:10.1271/bbb1961.53.2757
qualifier: involved_in
review:
summary: >-
Direct experimental (IDA) annotation of lignin catabolic process from the original LSD-I
characterization.
action: ACCEPT
reason: >-
Core biological process, experimentally supported (duplicate term from a distinct reference).
- term:
id: GO:0050054
label: lignostilbene alpha beta-dioxygenase activity
evidence_type: IDA
original_reference_id: DOI:10.1271/bbb1961.53.2757
qualifier: enables
review:
summary: >-
Direct experimental (IDA) annotation of lignostilbene alpha,beta-dioxygenase activity from the
original LSD-I purification and characterization.
action: ACCEPT
reason: >-
Core catalytic function, experimentally supported (the founding LSD-I characterization).
core_functions:
- description: >-
Non-heme iron lignostilbene-alpha,beta-dioxygenase (EC 1.13.11.43): cleaves the interphenyl
Calpha-Cbeta double bond of lignostilbene with O2 to two molecules of vanillin, in lignin-derived
stilbene catabolism. GO:0050054 is the exact, experimentally-supported MF term (a sibling of the
resveratrol leaf GO:7770086, added by go-ontology PR #32332 merged 2026-07-17, and a child of the
proposed stilbene alpha,beta-dioxygenase grouping).
molecular_function:
id: GO:0050054
label: lignostilbene alpha beta-dioxygenase activity
directly_involved_in:
- id: GO:0046274
label: lignin catabolic process
supported_by:
- reference_id: PMID:7763880
supporting_text: >-
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas
suggested_questions:
- question: >-
Like LSD-III, LSD-I carries the correct specific IDA annotations yet also the contradictory
TreeGrafter carotenoid terms; should these be removed and the TreeGrafter rule corrected for the SCO
branch of the CCO family?
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: []
reference_review:
relevance: LOW
correctness: MISCITED
review_notes: >-
TreeGrafter propagated carotenoid dioxygenase activity and carotene catabolic process onto LSD-I,
a genuine lignostilbene dioxygenase - directly contradicting the gene's own experimental (IDA)
annotations.
- id: GO_REF:0000120
title: Combined Automated Annotation using Multiple IEA Methods
findings: []
- id: PMID:7763880
title: Structural and enzymatical comparison of lignostilbene-alpha,beta-dioxygenase
isozymes, I, II, and III, from Pseudomonas paucimobilis TMY1009.
findings:
- statement: >-
Three lignostilbene alpha,beta-dioxygenase isozymes (I, II, III) were purified and characterized
from Pseudomonas (Sphingomonas) paucimobilis TMY1009.
supporting_text: >-
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas
reference_review:
relevance: HIGH
correctness: VERIFIED
review_notes: >-
Comparison of the LSD isozymes; supports the IDA lignostilbene dioxygenase activity and lignin
catabolic process annotations for LSD-I. Abstract-only cache.
- id: DOI:10.1271/bbb1961.53.2757
title: Purification and some properties of lignostilbene-.ALPHA.,.BETA.-dioxygenase responsible
for the C.ALPHA.-C.BETA. cleavage of a diarylpropane type lignin model compound from Pseudomonas
sp. TMY1009.
findings: []
reference_review:
relevance: HIGH
correctness: VERIFIED
review_notes: >-
Original LSD-I purification/characterization; source of the IDA lignostilbene dioxygenase
activity, lignin catabolic process, and iron-binding annotations. Not cached (DOI, pre-PMC era).