dapE

UniProt ID: Q88MP5
Organism: Pseudomonas putida KT2440
Review Status: DRAFT
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Gene Description

dapE encodes the metallodependent succinyl-diaminopimelate desuccinylase (EC 3.5.1.18) that hydrolyzes N-succinyl-LL-diaminopimelate to LL-diaminopimelate and succinate in the succinylated route of L-lysine biosynthesis. Its proteobacterial DapE-specific family distinguishes it from related ArgE acetylornithine deacetylases.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0006526 L-arginine biosynthetic process
IEA
GO_REF:0000118
REMOVE
Summary: This TreeGrafter process call reflects related ArgE enzymes, not PSEPK DapE.
Reason: Q88MP5 has the DapE-specific reaction, pathway assignment, and NCBIfam:TIGR01246 signature.
GO:0008270 zinc ion binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: Zinc binding is valid catalytic-metal context for DapE.
Reason: The metallohydrolase annotation supports metal binding, which is secondary to substrate-specific catalysis.
GO:0008777 acetylornithine deacetylase activity
IEA
GO_REF:0000118
REMOVE
Summary: This activity belongs to related ArgE-family proteins.
Reason: Q88MP5 is assigned to the proteobacterial DapE subfamily and EC 3.5.1.18; no evidence supports acetylornithine as its physiological substrate.
GO:0009014 succinyl-diaminopimelate desuccinylase activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the defining DapE molecular function.
Reason: EC 3.5.1.18, HAMAP MF_01690, and NCBIfam:TIGR01246 support the same reaction. Support is the curated HAMAP rule's FUNCTION statement and the DapE family classifications (a rule-based, not experimental, assignment for Q88MP5).
Supporting Evidence:
file:PSEPK/dapE/dapE-uniprot.txt
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminopimelate (DAP)
file:PSEPK/dapE/dapE-uniprot.txt
HAMAP; MF_01690; DapE; 1.
file:PSEPK/dapE/dapE-uniprot.txt
NCBIfam; TIGR01246; dapE_proteo; 1.
GO:0009085 L-lysine biosynthetic process
IEA
GO_REF:0000002
ACCEPT
Summary: DapE deprotects LL-diaminopimelate in L-lysine biosynthesis.
Reason: UniProt assigns Q88MP5 to L-lysine biosynthesis via the DAP pathway.
GO:0016787 hydrolase activity
IEA
GO_REF:0000120
MARK AS OVER ANNOTATED
Summary: This generic hydrolase term is redundant with the specific DapE activity.
Reason: GO:0009014 captures the substrate-specific reaction.
GO:0050897 cobalt ion binding
IEA
GO_REF:0000104
KEEP AS NON CORE
Summary: Cobalt binding is plausible catalytic-metal context for DapE.
Reason: UniProt records cobalt for this metallohydrolase, but metal binding is secondary to catalysis.

Core Functions

Hydrolyzes N-succinyl-LL-diaminopimelate to LL-diaminopimelate and succinate in L-lysine biosynthesis.

Supporting Evidence:
  • file:PSEPK/dapE/dapE-uniprot.txt
    Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminopimelate (DAP)
  • file:PSEPK/dapE/dapE-uniprot.txt
    HAMAP; MF_01690; DapE; 1.

References

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Deep Research

OpenScientist

(dapE-deep-research-openscientist.md)

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