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). |
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Download this section (compressed HTML)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?
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