sad-II

UniProt ID: Q88I50
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
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Gene Description

sad-II (PP_3151) encodes a predicted succinate-semialdehyde dehydrogenase of the GabD1/Sad aldehyde-dehydrogenase family in Pseudomonas putida KT2440. It is expected to oxidize succinate semialdehyde to succinate with a nicotinamide nucleotide acceptor. Its measured NAD versus NADP preference and physiological substrate regime remain unresolved. PP_3151 is induced in a reported vanillin-response study and has been included in engineered multigene deletion strains, without an isolated assignment of vanillin turnover.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004030 aldehyde dehydrogenase [NAD(P)+] activity
IEA
GO_REF:0000002
MODIFY
Summary: The aldehyde-dehydrogenase substrate class is resolved to succinate-semialdehyde oxidation without selecting one nicotinamide cofactor.
Reason: PANTHER, the SSADH FunFam and GabD1-like CDD classification agree on succinate-semialdehyde oxidation. They are computational classifications, not independent target enzyme assays. For Sad-II, PTHR43217:SF1 is explicitly cofactor-general NAD(P), unlike the NADP-named Sad-I subgroup. It is compatible with the NAD-capacity FunFam but does not independently resolve acceptor preference. This is a substrate-specific semantic refinement to GO:0009013; live QuickGO does not currently place GO:0009013 below GO:0004030, so no is_a relationship between that pair is claimed. Neither the P. putida isoenzymes in PMID:3355840 nor Salmonella YneI in PMID:23229889 establishes a locus-specific 4HB, GABA or putrescine pathway.
Supporting Evidence:
file:PSEPK/sad-II/sad-II-uniprot.txt
FunFam; 3.40.605.10:FF:000012; NAD-dependent succinate-semialdehyde dehydrogenase; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
CDD; cd07100; ALDH_SSADH1_GabD1; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
GO:0004777 succinate-semialdehyde dehydrogenase (NAD+) activity
IEA
GO_REF:0000120
ACCEPT
Summary: PP_3151 retains a qualified NAD-capacity inference; its measured acceptor preference is unresolved.
Reason: The exact Q88I50 NAD-dependent SSADH FunFam supplies positive functional-family evidence for NAD capacity. For Sad-II, PTHR43217:SF1 is explicitly cofactor-general NAD(P), unlike the NADP-named Sad-I subgroup. It is compatible with the NAD-capacity FunFam but does not independently resolve acceptor preference. Retention of GO:0004777 is therefore a compatible family-level inference, not a measured target-specific cofactor assignment. The live GO definition describes NAD-supported catalysis and does not assert exclusive NAD use or absence of NADP activity. PMID:3355840 separates P. putida NAD-preferring and NADP-dependent isoenzymes but does not map either to this locus; Salmonella YneI promiscuity in PMID:23229889 is contextual, not a target assay. The ARBA-only NADP keyword is not used as independent evidence in either direction. The core and broad-term refinements retain cofactor-general SSADH chemistry rather than using this inference to settle physiological acceptor choice.
Supporting Evidence:
file:PSEPK/sad-II/sad-II-uniprot.txt
FunFam; 3.40.605.10:FF:000012; NAD-dependent succinate-semialdehyde dehydrogenase; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
CDD; cd07100; ALDH_SSADH1_GabD1; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
GO:0016491 oxidoreductase activity
IEA
GO_REF:0000002
MODIFY
Summary: The unspecified oxidoreductase reaction is resolved to succinate-semialdehyde oxidation without selecting one nicotinamide cofactor.
Reason: PANTHER, the SSADH FunFam and GabD1-like CDD classification agree on succinate-semialdehyde oxidation. They are computational classifications, not independent target enzyme assays. For Sad-II, PTHR43217:SF1 is explicitly cofactor-general NAD(P), unlike the NADP-named Sad-I subgroup. It is compatible with the NAD-capacity FunFam but does not independently resolve acceptor preference. GO:0009013 is a verified descendant of GO:0016491 and specifies the supported substrate while leaving NAD/NADP choice open. Neither the P. putida isoenzymes in PMID:3355840 nor Salmonella YneI in PMID:23229889 establishes a locus-specific 4HB, GABA or putrescine pathway.
Supporting Evidence:
file:PSEPK/sad-II/sad-II-uniprot.txt
FunFam; 3.40.605.10:FF:000012; NAD-dependent succinate-semialdehyde dehydrogenase; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
CDD; cd07100; ALDH_SSADH1_GabD1; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
IEA
GO_REF:0000117
MODIFY
Summary: The NAD(P)-linked aldehyde/oxo-donor reaction is resolved to succinate-semialdehyde oxidation without selecting one nicotinamide cofactor.
Reason: PANTHER, the SSADH FunFam and GabD1-like CDD classification agree on succinate-semialdehyde oxidation. They are computational classifications, not independent target enzyme assays. For Sad-II, PTHR43217:SF1 is explicitly cofactor-general NAD(P), unlike the NADP-named Sad-I subgroup. It is compatible with the NAD-capacity FunFam but does not independently resolve acceptor preference. GO:0009013 is a verified descendant of GO:0016620 and specifies the supported substrate while leaving NAD/NADP choice open. Neither the P. putida isoenzymes in PMID:3355840 nor Salmonella YneI in PMID:23229889 establishes a locus-specific 4HB, GABA or putrescine pathway.
Supporting Evidence:
file:PSEPK/sad-II/sad-II-uniprot.txt
FunFam; 3.40.605.10:FF:000012; NAD-dependent succinate-semialdehyde dehydrogenase; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
CDD; cd07100; ALDH_SSADH1_GabD1; 1.
file:PSEPK/sad-II/sad-II-uniprot.txt
PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.

Core Functions

Predicted succinate-semialdehyde oxidation to succinate by PP_3151, supported by concordant substrate-family classifications. NAD capacity is retained as a qualified FunFam-based inference, but measured cofactor preference and native pathway allocation remain unresolved. The core uses cofactor-general chemistry and is not an assertion that both acceptors have been experimentally tested.

Supporting Evidence:
  • file:PSEPK/sad-II/sad-II-uniprot.txt
    FunFam; 3.40.605.10:FF:000012; NAD-dependent succinate-semialdehyde dehydrogenase; 1.
  • file:PSEPK/sad-II/sad-II-uniprot.txt
    CDD; cd07100; ALDH_SSADH1_GabD1; 1.
  • file:PSEPK/sad-II/sad-II-uniprot.txt
    PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.

References

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Suggested Questions for Experts

Q: Which substrate regime distinguishes the physiological role of Sad-II from Sad-I and GabD-II?

Q: Does purified PP_3151 accept both NAD and NADP, and are their catalytic efficiencies consistent with the NAD-dependent functional-family assignment?

Suggested Experiments

Experiment: Compare sad-II single and combinatorial deletion phenotypes, expression, and NAD- versus NADP-linked activity during growth on 4-hydroxyphenylacetate, putrescine, 4-hydroxybutyrate, and GABA.

Hypothesis: Sad-II contributes to one of the substrate-induced P. putida SSADH activities and has a physiological regime distinct from Sad-I and GabD-II.

Deep Research

OpenScientist

(sad-II-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(sad-II-notes.md)

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