GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

ARBA supplied broad enzyme-class and aromatic catabolism process annotations that need specificity review.

GO_REF:0000120

Combined automated GO annotation using multiple IEA methods

Automated EC/Rhea mapping supplies the GalC aldolase molecular-function term.

file:PSEPK/galC/galC-uniprot.txt

UniProtKB reviewed entry for galC

UniProt identifies GalC as the CHA aldolase in gallate degradation, converting CHA to pyruvate and oxaloacetate.

PMID:21219457

Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida

The KT2440 gal cluster paper identifies GalC as the aldolase catalyzing CHA cleavage.

file:PSEPK/galC/galC-deep-research-falcon.md

Falcon (Edison Scientific) deep research report for galC (Pseudomonas putida KT2440)

GalC is the CHA (HMG/CHA) aldolase that cleaves CHA to pyruvate and oxaloacetate, the terminal carbon-splitting step of gallate catabolism.

"GalC is identified as the **HMG/CHA aldolase** responsible for converting CHA into the TCA-cycle metabolites **pyruvate and oxaloacetate**"
GalC is the terminal carbon-carbon cleavage step of the gallate pathway, completing conversion of an aromatic compound into central metabolism.

"GalC is the terminal carbon–carbon cleavage step that converts the ring-cleavage-derived intermediate (CHA) into **pyruvate + oxaloacetate**, thereby completing conversion of an aromatic compound into central metabolism"
GalC belongs to the class II, divalent metal-dependent pyruvate aldolases and uses an enolate (not Schiff-base) mechanism.

"HMG/CHA aldolases as **class II, divalent metal-dependent pyruvate aldolases**, operating via an **enolate** mechanism (not a Schiff-base)"
The enzyme is divalent-metal dependent, with Mg2+ featuring in structural discussion and conserved acidic motifs supporting metal binding.

"The enzyme is described as **divalent-metal dependent**; Mg2+ appears in structural discussion"
HMG/CHA aldolases show a secondary oxaloacetate decarboxylase activity, consistent with a shared pyruvate-enolate intermediate.

"HMG/CHA aldolases are reported to show **secondary oxaloacetate decarboxylase activity**, rationalized by a shared pyruvate-enolate intermediate"
GalC adopts an RraA-like fold, consistent with its UniProt LigK/PcmE family and RraA-like domain assignment.

"A solved structure (discussed for *Pseudomonas putida* F1 homologs) shows an **αββα sandwich fold** that is **structurally similar to RraA family proteins**"
GalC is a soluble metabolic enzyme acting intracellularly (likely cytosolic) on cytosolic intermediates.

"the most defensible annotation from these sources is that GalC functions **intracellularly (likely cytosolic)** as part of central aromatic catabolism"
GalC functions within the KT2440 gallate-utilization gene cluster galDCBRPAT.

"A KT2440 gallate-utilization gene cluster is described as **galDCBRPAT**, encoding enzymatic steps for gallate catabolism plus uptake/regulation"

file:PSEPK/galC/galC-deep-research-openscientist.md

OpenScientist deep research report for galC (Pseudomonas putida KT2440)

The report corroborates the direct PMID:21219457 assignment of GalC as the terminal CHA aldolase while explicitly identifying untested structural, localization, and side-activity claims as knowledge gaps.

"No direct crystal structure or purified kinetics of GalC itself."