aldB-I

UniProt ID: Q88QE9
Organism: Pseudomonas putida KT2440
Review Status: DRAFT
Aliases:
PP_0545
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Gene Description

AldB-I (PP_0545) is a soluble, non-acylating NAD-dependent aldehyde dehydrogenase of the AldB/AcoD-like family. Its position immediately beside the ethanolamine transporter and eutBC makes oxidation of EutBC-derived acetaldehyde to acetate a strong physiological hypothesis, but direct KT2440 substrate-specific or pathway evidence is not yet available.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004029 aldehyde dehydrogenase (NAD+) activity
IEA
GO_REF:0000003 		ACCEPT
Summary: EC 1.2.1.3 and the AldB/AcoD-like family support NAD-dependent aldehyde oxidation.
Reason: This is the substrate-generic NAD-dependent ALDH activity. The EC 1.2.1.3 in the record is a submitter import and is not used as evidence; the support is family classification. Q88QE9 carries the Pfam PF00171 aldehyde dehydrogenase domain and both PROSITE ALDH active-site signatures, and matches the NCBIfam NF050026 (AcaldDHExaC) and CDD cd07559 (ALDH_ACDHII_AcoD-like) models, whose characterized exemplar, Pseudomonas aeruginosa ExaC, is an NAD(+)-dependent acetaldehyde dehydrogenase (PMID:10075429). The NAD+ specificity is therefore inferred from that family exemplar, not measured for AldB-I. Locus adjacency does not establish acetaldehyde as the preferred substrate.
Supporting Evidence:
file:PSEPK/aldB-I/aldB-I-uniprot.txt
DR NCBIfam; NF050026; AcaldDHExaC; 1.
file:PSEPK/aldB-I/aldB-I-uniprot.txt
DR CDD; cd07559; ALDH_ACDHII_AcoD-like; 1.
file:PSEPK/aldB-I/aldB-I-uniprot.txt
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PMID:10075429
An ORF encoding a NAD(+)-dependent acetaldehyde dehydrogenase (exaC) was located downstream of the cytochrome c550 gene and in the same orientation.
GO:0004030 aldehyde dehydrogenase [NAD(P)+] activity
IEA
GO_REF:0000117 		MODIFY
Summary: The ARBA term leaves cofactor specificity ambiguous despite the EC 1.2.1.3 assignment.
Reason: UniProt EC mapping supports the NAD+-specific child GO:0004029, but does not establish a specific aldehyde substrate.
Supporting Evidence:
file:PSEPK/aldB-I/aldB-I-uniprot.txt
EC=1.2.1.3
GO:0016491 oxidoreductase activity
IEA
GO_REF:0000002 		MARK AS OVER ANNOTATED
Summary: This broad InterPro parent adds no information beyond the specific aldehyde-dehydrogenase chemistry.
Reason: Retain the more informative NAD-dependent aldehyde-dehydrogenase term as the core annotation.

Core Functions

Non-acylating NAD-dependent aldehyde oxidation. Oxidation of the acetaldehyde generated by adjacent EutBC is a pathway hypothesis, not an established substrate assignment for KT2440 AldB-I.

Molecular Function:
aldehyde dehydrogenase (NAD+) activity
Supporting Evidence:
  • file:PSEPK/aldB-I/aldB-I-uniprot.txt
    DR NCBIfam; NF050026; AcaldDHExaC; 1.
  • file:PSEPK/aldB-I/aldB-I-uniprot.txt
    DR Pfam; PF00171; Aldedh; 1.
  • PMID:10075429
    An ORF encoding a NAD(+)-dependent acetaldehyde dehydrogenase (exaC) was located downstream of the cytochrome c550 gene and in the same orientation.

References

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Suggested Questions for Experts

Q: Is acetaldehyde the preferred physiological substrate of AldB-I, which would support GO:0140087, and is PP_0545 required for ethanolamine-supported growth?

Suggested Experiments

Experiment: Measure AldB-I kinetics with acetaldehyde and alternative aldehydes, then test ethanolamine growth in an aldB-I deletion/complementation series.

Type: enzyme kinetics and reverse genetics

Deep Research

Asta

(aldB-I-deep-research-asta.md)

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📚 Additional Documentation

Notes

(aldB-I-notes.md)

aldB-I curation notes

  • Q88QE9 / PP_0545 is PTHR43111:SF1, the AldB/AcoD-like family. Pseudomonas ExaC Q9ZAA1 is a verified family exemplar.
  • AldB-I is not classical acetylating EutE: EutE is PTHR11699/IPR012408 and catalyzes acetyl-CoA formation, whereas AldB-I is a 506-aa non-acylating EC 1.2.1.3 enzyme predicted to form acetate.
  • All three QuickGO rows were reviewed. GO:0004029 is retained as the supported core function; GO:0140087 and ethanolamine-process participation remain explicit hypotheses because adjacency alone does not establish substrate preference.
  • No completed OpenScientist artifact was present for aldB-I. Existing Asta retrieval was sparse and not used as primary evidence.

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