Cytochrome b556 membrane anchor subunit of the succinate dehydrogenase/respiratory Complex II enzyme in Pseudomonas putida KT2440. SdhC is a multi-pass inner-membrane protein that, together with SdhD, anchors the SdhAB catalytic head to the plasma membrane and forms the membrane electron-transfer/quinone-interaction domain. It supports the succinate-to-fumarate TCA-cycle step and respiratory quinone reduction by the SdhABCD complex.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Correct localization for the bacterial inner-membrane succinate dehydrogenase cytochrome b subunit. Reason: The UniProt SUBCELLULAR LOCATION line rests only on an ARBA rule, so the location is argued from sequence analysis and family membership instead. Phobius predicts three transmembrane helices (FT TRANSMEM 28..49, 69..86, 107..127), and Q88FA5 matches the succinate dehydrogenase cytochrome b556 family (NCBIfam TIGR02970, Pfam PF01127 Sdh_cyt), whose members are the membrane anchor of Complex II. Alpha-helical multi-pass proteins of a Gram-negative bacterium reside in the inner membrane, which corresponds to the GO plasma membrane. Supporting Evidence: file:PSEPK/sdhC/sdhC-uniprot.txt TRANSMEM 28..49 file:PSEPK/sdhC/sdhC-uniprot.txt DR NCBIfam; TIGR02970; succ_dehyd_cytB; 1. |
| GO:0006099 tricarboxylic acid cycle | IEA GO_REF:0000002 | ACCEPT | Summary: Correct TCA-cycle annotation because SdhC is part of the SdhABCD succinate dehydrogenase complex. Reason: The SdhABCD complex catalyzes the succinate-to-fumarate step of the TCA cycle, and SdhC is a membrane anchor/cytochrome b subunit of this required complex. The UniProt PATHWAY line is ARBA-only and is not used; the support is family membership - Q88FA5 matches the succinate dehydrogenase cytochrome b556 models (NCBIfam TIGR02970, CDD cd03499 SQR_TypeC_SdhC) - and the curated PIRSR heme note placing the heme between the two transmembrane subunits of the complex. No KT2440 sdhC mutant data are cached. Supporting Evidence: file:PSEPK/sdhC/sdhC-uniprot.txt DR NCBIfam; TIGR02970; succ_dehyd_cytB; 1. file:PSEPK/sdhC/sdhC-uniprot.txt DR CDD; cd03499; SQR_TypeC_SdhC; 1. file:PSEPK/sdhC/sdhC-uniprot.txt Note=The heme is bound between the two transmembrane subunits. |
| GO:0009055 electron transfer activity | IEA GO_REF:0000002 | ACCEPT | Summary: Correct subunit-level role for the cytochrome b membrane domain of succinate dehydrogenase. Reason: SdhC is the cytochrome b556 membrane subunit of Complex II and contains heme-binding features; it contributes to electron transfer/quinone reduction by the holoenzyme. Supporting Evidence: file:PSEPK/sdhC/sdhC-uniprot.txt Name=heme; Xref=ChEBI:CHEBI:30413; |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Correct but less precise than the plasma membrane/inner membrane annotation. Reason: SdhC is a membrane protein, but UniProt specifies the bacterial cell inner membrane and GOA already has the more informative plasma membrane annotation. Use GO:0005886 as the preferred location term. Proposed replacements: plasma membrane Supporting Evidence: file:PSEPK/sdhC/sdhC-uniprot.txt SUBCELLULAR LOCATION: Cell inner membrane |
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Download this section (compressed HTML)Q: Does SdhC provide the main cytochrome b/heme coordination site in the P. putida KT2440 Complex II membrane domain, and how does it cooperate with SdhD in quinone reduction?
Experiment: Mutate predicted SdhC heme-coordinating residues and assay SdhABCD heme content, quinone binding, membrane assembly, and succinate:quinone activity.
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Download this section (compressed HTML)The sdhC OpenScientist report identified Q88FA5/PP_4193 as the cytochrome b556
membrane-anchor subunit of SdhABCD Complex II, with the detailed heme- and
quinone-site claims transferred from E. coli and other characterized homologs.
I used it only as homology- and operon-level corroboration for the KT2440
subunit identity, not as direct P. putida KT2440 biochemical evidence.
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