YAH1 (YPL252C) encodes the essential mitochondrial adrenodoxin-type [2Fe-2S] ferredoxin of S. cerevisiae. Located in the mitochondrial matrix, Yah1 is reduced by the NADPH-dependent ferredoxin reductase Arh1 and passes single electrons to several acceptors. It is required for de novo [2Fe-2S] cluster synthesis on the Isu1 scaffold (and hence for maturation of both mitochondrial and cytosolic Fe-S proteins), for the Cox15-catalysed hydroxylation of heme O to heme A, and for coenzyme Q6 biosynthesis, where it is the probable electron donor for the Coq6 ring hydroxylation. Depletion of Yah1 causes mitochondrial iron accumulation and loss of Fe-S protein activities.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: IBA mitochondrion from the adrenodoxin-type ferredoxin node (plant, mammalian and yeast members). Reason: Correct; matrix is the precise compartment. Supporting Evidence: PMID:10375636 We show that the protein is targeted to the mitochondrial matrix |
| GO:0005739 mitochondrion | NAS PMID:26342079 Mapping Key Residues of ISD11 Critical for NFS1-ISD11 Subcom... | ACCEPT | Summary: ComplexPortal NAS for the mitochondrial ISC assembly complex citing an ISD11/NFS1 study. Reason: Correct location (redundant with matrix IDA). Supporting Evidence: PMID:26342079 In mammalian mitochondria, the initial step of the Fe-S cluster assembly process is assisted by the NFS1-ISD11 complex |
| GO:0005759 mitochondrial matrix | EXP PMID:10655482 A mitochondrial ferredoxin is essential for biogenesis of ce... | ACCEPT | Summary: Lange et al. located Yah1p in the mitochondrial matrix (UniProt EXP). Reason: Correct. Supporting Evidence: PMID:10655482 we identify the essential ferredoxin Yah1p of Saccharomyces cerevisiae mitochondria as a central component of the Fe/S protein biosynthesis machinery |
| GO:0005759 mitochondrial matrix | IDA PMID:10375636 YAH1 of Saccharomyces cerevisiae: a new essential gene that ... | ACCEPT | Summary: Barros & Nobrega showed Yah1 is targeted to the mitochondrial matrix. Reason: Direct evidence. Supporting Evidence: PMID:10375636 We show that the protein is targeted to the mitochondrial matrix |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location mapping (SL-0170). Reason: Correct. Supporting Evidence: PMID:10375636 We show that the protein is targeted to the mitochondrial matrix |
| GO:0006744 ubiquinone biosynthetic process | IMP PMID:20534343 Involvement of mitochondrial ferredoxin and para-aminobenzoi... | ACCEPT | Summary: Gal-YAH1 depletion blocks Q6 synthesis with accumulation of 3-hexaprenyl-4-hydroxyphenol and -aminophenol, implicating Yah1 in the first ring hydroxylation. Reason: Yah1 supplies the reducing equivalents consumed by the Coq6 (and likely C1) hydroxylation, so it contributes to a chemical step rather than being merely required. Supporting Evidence: PMID:20534343 the mitochondrial ferredoxin Yah1p and the ferredoxin reductase Arh1p are required for Q(6) biosynthesis, probably for the first hydroxylation of the pathway |
| GO:0006744 ubiquinone biosynthetic process | IMP PMID:21944752 Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxy... | ACCEPT | Summary: Ozeir et al. propose Yah1/Arh1 as the in vivo electron source for Coq6 C5 hydroxylation. Reason: As above. Supporting Evidence: PMID:21944752 the ferredoxin Yah1 and the ferredoxin reductase Arh1 may be the in vivo source of electrons for Coq6 |
| GO:0006784 heme A biosynthetic process | IGI PMID:11788607 Mitochondrial ferredoxin is required for heme A synthesis in... | ACCEPT | Summary: Genetic interaction with COX15 overexpression: heme A increases more when Cox15p and ferredoxin are co-overexpressed. Reason: Yah1 is the electron donor for the Cox15 heme O hydroxylation; direct participant. Supporting Evidence: PMID:11788607 three lines of evidence confirm a requirement of ferredoxin in heme A synthesis PMID:11788607 a three-component monooxygenase consisting of Cox15p, ferredoxin, and ferredoxin reductase |
| GO:0006784 heme A biosynthetic process | IMP PMID:11788607 Mitochondrial ferredoxin is required for heme A synthesis in... | ACCEPT | Summary: Temperature-conditional yah1 mutants show reduced heme A relative to heme B and reduced label incorporation into heme A. Reason: Direct genetic evidence. Supporting Evidence: PMID:11788607 three lines of evidence confirm a requirement of ferredoxin in heme A synthesis |
| GO:0009055 electron transfer activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA electron transfer activity from the adrenodoxin family node (bovine/human adrenodoxins and others). Reason: Core function of a [2Fe-2S] ferredoxin. Supporting Evidence: PMID:10375636 Adrenodoxin is the second electron carrier that participates in a mitochondrial electron transfer chain file:yeast/YAH1/YAH1-uniprot.txt Transfers electrons |
| GO:0009055 electron transfer activity | NAS PMID:10375636 YAH1 of Saccharomyces cerevisiae: a new essential gene that ... | ACCEPT | Summary: Statement that Yah1, as an adrenodoxin homolog, is an electron carrier of a mitochondrial electron transfer chain. Reason: Correct; supported experimentally by later studies. Supporting Evidence: PMID:10375636 Adrenodoxin is the second electron carrier that participates in a mitochondrial electron transfer chain |
| GO:0016226 iron-sulfur cluster assembly | IDA PMID:10655482 A mitochondrial ferredoxin is essential for biogenesis of ce... | ACCEPT | Summary: Yah1 depletion abolishes assembly of mitochondrial and cytosolic Fe/S proteins and causes mitochondrial iron accumulation. Reason: Core process; Yah1 supplies electrons for cluster formation on Isu1. Supporting Evidence: PMID:10655482 we identify the essential ferredoxin Yah1p of Saccharomyces cerevisiae mitochondria as a central component of the Fe/S protein biosynthesis machinery PMID:10655482 Yah1p was shown to be required for the assembly of Fe/S proteins both inside mitochondria and in the cytosol |
| GO:0016226 iron-sulfur cluster assembly | IMP PMID:12970193 Components involved in assembly and dislocation of iron-sulf... | ACCEPT | Summary: Yah1 depletion strongly decreases de novo Fe/S cluster synthesis on the Isu1 scaffold. Reason: Direct evidence for the ISC step. Supporting Evidence: PMID:12970193 Depletion of the cysteine desulfurase Nfs1p, the ferredoxin Yah1p or the yeast frataxin homologue Yfh1p by regulated gene expression causes a strong decrease in the de novo synthesis of Fe/S clusters on Isu1p |
| GO:0016226 iron-sulfur cluster assembly | NAS PMID:34199378 Molecular Details of the Frataxin-Scaffold Interaction durin... | ACCEPT | Summary: ComplexPortal NAS from a review of frataxin-scaffold interactions describing ferredoxin as the electron donor within the core ISC complex. Reason: Correct; redundant with experimental evidence. Supporting Evidence: PMID:34199378 Electrons are provided by a mitochondrial ferredoxin (FDX2 in humans) to form the overall NIAUFX complex |
| GO:0016653 oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor | IGI PMID:11788607 Mitochondrial ferredoxin is required for heme A synthesis in... | MODIFY | Summary: GO:0016653 describes catalysis in which NAD(P)H reduces a heme protein. That is the net activity of the three-component Arh1-Yah1-Cox15 system; Yah1 itself does not bind or oxidize NAD(P)H (Arh1 does) but carries electrons from Arh1 to Cox15. Reason: The finding (Yah1 required for electron supply to the heme-protein Cox15) is sound, but the MF belongs to the system/reductase; for the ferredoxin the correct activity is electron transfer. Proposed replacements: electron transfer activity Supporting Evidence: PMID:11788607 a three-component monooxygenase consisting of Cox15p, ferredoxin, and ferredoxin reductase file:yeast/YAH1/YAH1-uniprot.txt Transfers electrons |
| GO:0016653 oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor | IMP PMID:11788607 Mitochondrial ferredoxin is required for heme A synthesis in... | MODIFY | Summary: Same paper, mutant phenotype: yah1-ts reduces heme A. As above, the NAD(P)H-oxidizing step is carried out by Arh1, not Yah1. Reason: Replace with electron transfer activity for the ferredoxin. Proposed replacements: electron transfer activity Supporting Evidence: PMID:11788607 three lines of evidence confirm a requirement of ferredoxin in heme A synthesis PMID:11788607 a three-component monooxygenase consisting of Cox15p, ferredoxin, and ferredoxin reductase |
| GO:0022900 electron transport chain | IBA GO_REF:0000033 | ACCEPT | Summary: IBA electron transport chain from the adrenodoxin family. GO:0022900 is defined generically (carriers transferring electrons to terminal acceptors), which fits the NADPH-Arh1-Yah1-acceptor chain. Reason: Appropriate under the current generic definition, though less informative than the specific processes (Fe-S assembly, heme A, CoQ). Supporting Evidence: PMID:10375636 Adrenodoxin is the second electron carrier that participates in a mitochondrial electron transfer chain |
| GO:0051536 iron-sulfur cluster binding | IDA PMID:31040179 Mitochondria export iron-sulfur and sulfur intermediates to ... | ACCEPT | Summary: UniProt IDA from Pandey et al. 2019 (Fe-S intermediate export). The cached abstract does not mention Yah1; the curator presumably used Yah1 Fe-S loading data in the full text. Yah1 is an established [2Fe-2S] protein. Reason: Deferring to the curator; the binding is well established. GO:0051537 is more precise. Supporting Evidence: file:yeast/YAH1/YAH1-uniprot.txt Note=Binds 1 [2Fe-2S] cluster. |
| GO:0051536 iron-sulfur cluster binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO from 2Fe-2S ferredoxin domain entries. Reason: Correct, though GO:0051537 is more precise. Supporting Evidence: file:yeast/YAH1/YAH1-uniprot.txt Note=Binds 1 [2Fe-2S] cluster. |
| GO:0051537 2 iron, 2 sulfur cluster binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO 2Fe-2S cluster binding from the adrenodoxin-type ferredoxin signatures (IPR001055/IPR018298). Reason: Correct and specific; Yah1 binds one [2Fe-2S] cluster. Supporting Evidence: file:yeast/YAH1/YAH1-uniprot.txt Note=Binds 1 [2Fe-2S] cluster. |
| GO:0140647 P450-containing electron transport chain | IEA GO_REF:0000002 | REMOVE | Summary: InterPro2GO P450-containing electron transport chain from the adrenodoxin signature. Vertebrate adrenodoxins feed mitochondrial P450s, but S. cerevisiae has no mitochondrial cytochrome P450; Yah1 feeds Cox15, Coq6 and the ISC machinery. Reason: The InterPro mapping over-propagates a vertebrate-specific role; there is no P450 acceptor in yeast mitochondria. Supporting Evidence: PMID:9727014 to date, no mitochondrial cytochrome P450 has been identified PMID:11788607 a three-component monooxygenase consisting of Cox15p, ferredoxin, and ferredoxin reductase |
| GO:1990229 iron-sulfur cluster assembly complex | NAS PMID:34199378 Molecular Details of the Frataxin-Scaffold Interaction durin... | KEEP AS NON CORE | Summary: ComplexPortal includes the ferredoxin in the mitochondrial ISC assembly complex (NIAUFX in humans). Yah1 interacts with Isu1 in its reduced state to deliver electrons. Reason: Yah1 associates transiently with the core ISC complex as an electron donor; reasonable but not a stable subunit. Supporting Evidence: PMID:34199378 Electrons are provided by a mitochondrial ferredoxin (FDX2 in humans) to form the overall NIAUFX complex file:yeast/YAH1/YAH1-uniprot.txt Interacts in its reduced state with the apo form of ISU1. |
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Download this section (compressed HTML)Ferredoxin of the mitochondrial matrix; required for formation of cellular iron-sulfur proteins; involved in heme A biosynthesis; human homolog FDX1L can complement yeast by allowing growth during down-regulation of yeast YAH1
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