dapB

UniProt ID: Q88DU4
Organism: Pseudomonas putida KT2440
Review Status: DRAFT
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Gene Description

dapB encodes 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8), which reduces the DapA product to tetrahydrodipicolinate in the second dedicated reaction of the diaminopimelate route to L-lysine. DapB-family enzymes can use NADPH or NADH as the reducing cofactor.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005737 cytoplasm
IEA
GO_REF:0000120
KEEP AS NON CORE
Summary: DapB is a soluble cytoplasmic biosynthetic enzyme.
Reason: The location is valid but secondary to the reaction.
GO:0005829 cytosol
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: This duplicates the retained bacterial cytoplasm annotation.
Reason: Relaxed from MARK_AS_OVER_ANNOTATED on re-review, per the rule that broad-but-true terms are not over-annotations. DapB is a soluble cytoplasmic enzyme with no signal peptide, transmembrane segment or lipobox, so the cytosol is where it resides; carrying the broader cytoplasm term on another row makes this one redundant, not incorrect.
GO:0008839 4-hydroxy-tetrahydrodipicolinate reductase activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the defining DapB molecular function.
Reason: The HAMAP MF_00102 curated function statement and DapB family membership (HAMAP, NCBIfam TIGR00036) agree on HTPA reduction; this is a family-rule inference, as Q88DU4 itself has not been assayed.
Supporting Evidence:
file:PSEPK/dapB/dapB-uniprot.txt
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
file:PSEPK/dapB/dapB-uniprot.txt
DR NCBIfam; TIGR00036; dapB; 1.
GO:0009085 L-lysine biosynthetic process
IEA
GO_REF:0000002
ACCEPT
Summary: DapB performs the reduction step of the lysine DAP pathway.
Reason: UniProt assigns Q88DU4 to L-lysine biosynthesis via the DAP pathway.
GO:0016726 oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
IEA
GO_REF:0000104
MARK AS OVER ANNOTATED
Summary: This broad redox term is redundant with the specific DapB activity.
Reason: GO:0008839 captures the substrate-specific reaction.
GO:0050661 NADP binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: NADP binding is valid cofactor context for DapB.
Reason: The reviewed reaction permits NADPH, but cofactor binding is less informative than catalysis.
GO:0051287 NAD binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: NAD binding is valid cofactor context for DapB.
Reason: The reviewed reaction permits NADH, but cofactor binding is less informative than catalysis.

Core Functions

Reduces 4-hydroxy-tetrahydrodipicolinate to tetrahydrodipicolinate in L-lysine biosynthesis.

Supporting Evidence:
  • file:PSEPK/dapB/dapB-uniprot.txt
    Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate
  • file:PSEPK/dapB/dapB-uniprot.txt
    DR HAMAP; MF_00102; DapB; 1.

References

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Knowledge Gaps

What is not known β€” curated, literature-grounded statements of the open unknowns (the inverse of core functions).

Gap: Q88DU4 has not been assayed directly, so its cofactor preference, kinetics, and physiological contribution have not been established in KT2440.

BIOLOGYCURATION

What is known: The exact reaction and dual NADPH/NADH capability are strongly supported by the reviewed record and conserved DapB-family evidence; target-specific quantitative properties remain inference-based.

Provenance (the field's own admissions):

Deep Research

OpenScientist

(dapB-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(dapB-notes.md)

Gene curation notes

2026-07-17 OpenScientist retrieval

The gene-level OpenScientist request for Q88DU4/PP_4725 reached the provider's
3600-second ceiling, was cancelled, and produced no report. No provider-named
deep-research file was created. This first-pass review therefore remains
grounded in the exact UniProt and GOA records, DapB-specific HAMAP and NCBIfam
assignments, Rhea reaction mappings, and the curated lysine-pathway context.
Direct biochemical or genetic evidence for this specific KT2440 protein was not
established in this pass.

πŸ“„ View Raw YAML

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