qmoA

Summary: Keyword-mapped oxidoreductase activity. QmoA is an HdrA-like iron-sulfur flavoprotein of the QmoABC electron-transfer complex.

Reason: QmoA is a redox subunit of the QmoABC complex, an HdrA-like flavoprotein with FAD/NAD-binding architecture (IPR036188, IPR039650). The general term is accurate; the specific physiological reaction of QmoA is not yet established, so no more specific child term is justified. Ramos et al. call QmoA a flavoprotein, and the complex binds two FAD groups, but no FAD-binding term is proposed for QmoA: unlike QmoB (Q72DT0), its UniProt record has no FAD cofactor line or FAD keyword, only FAD/NAD-binding domain hits, and the literature does not assign the two FADs to individual subunits.

Summary: Keyword-mapped metal ion binding, reflecting the iron of the protein's iron-sulfur cofactor.

Reason: QmoA is described as an iron-sulfur flavoprotein; iron binding is accurate though less informative than the 4Fe-4S cluster binding annotation.

Summary: Keyword-mapped iron-sulfur cluster binding.

Reason: QmoA is an iron-sulfur flavoprotein homologous to HdrA; the QmoABC subunits collectively carry two hemes b, two FAD groups and several iron-sulfur centers.

Summary: Keyword-mapped 4Fe-4S cluster binding (UniProt KW 4Fe-4S, ARBA).

Reason: QmoA is an HdrA-like iron-sulfur flavoprotein; HdrA-family proteins carry [4Fe-4S] clusters and the UniProt ARBA rule assigns 4Fe-4S. No PROSITE ferredoxin-type domain is called on this 412-residue protein, so the cluster type rests on family inference rather than a characterized site.

Summary: AP-MS interactome of D. vulgaris; UniProt records the QmoA (DVU_0848) - QmoB (DVU_0849) interaction from this work.

Reason: The interaction is real and expected: QmoA and QmoB are the two cytoplasmic subunits of the QmoABC complex. "Protein binding" is uninformative; the functional content is QmoA's electron-transfer role within the Qmo complex.

Proposed replacements: electron transfer activity

Summary: Tagless copurification in D. vulgaris; supports the QmoA-QmoB association and, in the same study, a Qmo - APS reductase alpha subunit association.

Reason: Same as the PMID:26873250 row: the interaction reflects QmoABC complex membership. "Protein binding" is uninformative; the functional content is electron transfer within the Qmo complex and toward AprAB.

Proposed replacements: electron transfer activity

Summary: QmoA is the QmoABC subunit that contacts APS reductase (AprAB), the enzyme that reduces APS to sulfite in dissimilatory sulfate reduction, and the qmoABC genes are required for growth with sulfate as electron acceptor.

Reason: Participation, not only necessity: QmoA is part of the electron-transfer complex proposed to deliver reducing equivalents to AprAB (an electron donor to a pathway step), and it is the Qmo subunit that physically interacts with AprAB. This replaces an earlier NEW proposal of GO:0019645 anaerobic electron transport chain, which was grounded only in a deep research file that misassigned DVU_0848 to the FlxABCD-HdrABC locus. Dropping it here rests on that sourcing, not on a judgement that the term is wrong for the complex. QmoC (Q72DS9), the membrane subunit that exchanges electrons with menaquinone, keeps GO:0019645 in its own review. Evidence code TAS because the qmoABC deletion phenotype (Zane et al. 2010) is reported here via Ramos et al. 2012, which also provides direct QmoA-AprAB interaction data.