GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:PSEPK/sad-II/sad-II-uniprot.txt

UniProt entry Q88I50 for sad-II

Independent domain and functional-family classifications support the retained enzyme class; submitted names, EC labels, electronic GO lines and ARBA-only statements are not used as independent functional evidence.
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.

"PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1."

PMID:23229889

Structure and activity of the NAD(P)+-dependent succinate semialdehyde dehydrogenase YneI from Salmonella typhimurium.

Salmonella YneI accepts both NAD and NADP; the abstract reports higher affinity for NAD. This establishes homolog chemistry, not the target protein kinetics.

"YneI can use both NAD(+) and NADP(+) as cofactors"

PMID:3355840

Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putida.

P. putida contains separable NAD-preferring/4-hydroxyphenylacetate-induced and NADP-dependent/putrescine-induced SSADH activities, without a locus assignment.

"Under standard assay conditions this enzyme acts preferentially with NAD but reduces NADP at 9% of the rate observed for NAD."

file:PSEPK/sad-II/sad-II-deep-research-openscientist.md

OpenScientist deep-research report for sad-II

The provider proposes a Sad/YneI-like assignment for Q88I50 and a Lys159 cofactor-determinant mapping; these are research leads from its own alignment, not published locus-specific results.

file:modules/bacterial_4_hydroxybutyrate_oxidation-deep-research-openscientist.md

OpenScientist review of bacterial 4-hydroxybutyrate oxidation

The report treats Sad-family enzymes as NAD-preferring but potentially cofactor-promiscuous.

file:PSEPK/sad-II/sad-II-notes.md

Manual evidence notes for sad-II

Append-only manual notes distinguish target evidence, homolog inference and unresolved pathway assignments.

PMID:40410945

Production of Vanillin From Ferulic Acid by Pseudomonas putida KT2440 Using Metabolic Engineering and In Situ Product Recovery.

PP_3151 is included among multiple deletions in vanillin-production strains, with target selection motivated by reported induction. These experiments do not isolate Sad-II turnover or establish its cofactor preference.

"protein abundance of PP_3151, PP_5120, and PP_5258"

PMID:25026441

Comprehensive proteome analysis of the response of Pseudomonas putida KT2440 to the flavor compound vanillin.

The vanillin-response proteomics study provides the upstream lead cited by the later multigene engineering study.

PMID:32256468

Unraveling 1,4-Butanediol Metabolism in Pseudomonas putida KT2440.

KT2440 PP_2049 deletion abolishes growth on tested 4HB/1,4-BDO conditions, but direct 4HB biochemical assays were unsuccessful; the paper retains competing routes. PP_3151 is an annotated downstream candidate, not an isolated enzyme assay.

"Attempts to obtain direct biochemical evidence for the oxidation hypothesis with dehydrogenase assays on whole cell extracts"