sucA

Summary: Correct E1 activity for the 2-oxoglutarate dehydrogenase complex.

Reason: No direct purified-enzyme assay exists for PP_4189 itself; the support is family membership. Q88FA9 matches the TIGR00239 2-oxoglutarate dehydrogenase E1 family model, the PIRSF000157 Oxoglu_dh_E1 family and InterPro IPR011603, whose characterized members (e.g. E. coli SucA) are the thiamine diphosphate-dependent OGDH E1 enzymes; this family membership is the argument for EC 1.2.4.2 activity. (PANTHER places it in subfamily PTHR23152:SF4, named for the 2-oxoadipate dehydrogenase E1, a closely related activity; the OGDH-specific TIGR00239/PIRSF models favour 2-oxoglutarate.) The UniProt function text (ARBA) and the EC line are predictions, and the sucA-sucB-lpdG neighborhood reported by the OpenScientist report is a lead, not cited as support.

Summary: Correct expected localization for a soluble bacterial OGDH E1 component.

Reason: The protein lacks secretion or membrane-anchor features and acts in the soluble bacterial OGDH complex; TreeGrafter records the cytosol term for this clade.

Summary: Correct TCA-cycle process annotation for the 2-oxoglutarate-to-succinyl-CoA step.

Reason: SucA is the E1 component of OGDH, which performs the 2-oxoglutarate oxidation step of the TCA cycle with SucB and an Lpd-family E3. The support is family membership (TIGR00239 and PIRSF000157 2-oxoglutarate dehydrogenase E1 models); the E1 catalyses the decarboxylation step itself, so it does part of the work of the cycle. No KT2440-specific assay is cached.

Summary: Correct but broad parent of the exact OGDH E1 activity.

Reason: The E1 subunit performs aldehyde or oxo-group oxidoreductase chemistry with the E2 lipoyl disulfide as acceptor, but GO:0004591 captures the specific substrate and complex context.

Summary: Correct cofactor binding for this thiamine diphosphate-dependent E1 component.

Reason: The OGDH E1 reaction is thiamine diphosphate dependent. Q88FA9 carries the thiamin diphosphate-binding fold (InterPro IPR029061, SUPFAM SSF52518) and matches the CDD TPP-dependent OGDC E1 model, which support ThDP binding by family/domain membership. (The UniProt COFACTOR line is an ARBA prediction and is not cited.)

Summary: Correct complex membership for the OGDH E1 component.

Reason: SucA belongs to the 2-oxoglutarate dehydrogenase E1 family (TIGR00239, PIRSF000157), whose members function only as the E1 subunit of the OGDH multienzyme complex; complex membership is argued from that family membership. The sucA-sucB-lpdG neighborhood (reported in the OpenScientist report) is consistent but is a lead, not cited as support. No KT2440 complex purification is cached.