Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
UniProt entry Q88K05 for sad-I
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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.
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For Sad-I, the NADP-named PTHR43217:SF2 subgroup is a substantive competing cofactor classification against the NAD-dependent FunFam. Neither is dismissed as experimental or privileged merely because it matches GOA.
"PANTHER; PTHR43217:SF2; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE [NADP(+)]; 1."
Structure and activity of the NAD(P)+-dependent succinate semialdehyde dehydrogenase YneI from Salmonella typhimurium.
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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"
Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putida.
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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."
OpenScientist deep-research report for sad-I
OpenScientist review of bacterial 4-hydroxybutyrate oxidation
Manual evidence notes for sad-I