thrC

UniProt ID: Q88MU7
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

thrC (PP_1471) encodes threonine synthase (EC 4.2.3.1), a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the final step of L-threonine biosynthesis, the conversion of O-phospho-L-homoserine and water to L-threonine and inorganic phosphate (RHEA:10840). The enzyme belongs to the threonine synthase family within the fold-type II (TrpB-like) PLP-dependent enzyme superfamily, with PLP bound as a Schiff base to an active-site lysine. As the committed terminal step of the aspartate-derived threonine biosynthetic branch, thrC supplies L-threonine for protein synthesis and downstream isoleucine biosynthesis in P. putida.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004795 threonine synthase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Core molecular function. This is the EC 4.2.3.1 activity (O-phospho-L-homoserine + H2O -> L-threonine + phosphate, RHEA:10840) matching the UniProt RecName, NCBIfam TIGR00260 (thrC) and threonine synthase family assignment (IPR004450). Well supported despite IEA evidence.
GO:0006520 amino acid metabolic process
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: Broad parent biological process term assigned by InterPro2GO from the Ser/Thr dehydratase PLP signature (IPR000634). It is correct but far less informative than the specific GO:0009088 (L-threonine biosynthetic process) that is also annotated. Marking as over-annotated relative to the precise child term.
GO:0009088 L-threonine biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: Core biological process. Threonine synthase catalyzes the terminal step of L-threonine biosynthesis; supported by the UniProt pathway annotation (UPA00050/UER00065) and UniRule. Accept.
GO:0030170 pyridoxal phosphate binding
IEA
GO_REF:0000002
ACCEPT
Summary: Supporting molecular function. Threonine synthase is PLP-dependent; the UniProt cofactor annotation lists pyridoxal 5'-phosphate and a Schiff-base lysine (MOD_RES at position 112) is documented. Accept.

Core Functions

PLP-dependent synthesis of L-threonine from O-phospho-L-homoserine, the terminal step of the aspartate-derived threonine biosynthetic pathway

Supporting Evidence:
  • GO_REF:0000120
    threonine synthase activity (EC:4.2.3.1, RHEA:10840) assigned to Q88MU7

References

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Deep Research

Asta

(thrC-deep-research-asta.md)

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