Adrenodoxin homolog, mitochondrial

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• 2 iron, 2 sulfur cluster binding Source: InterPro
• electron transfer activity Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • Ref.3

    "YAH1 of Saccharomyces cerevisiae: a new essential gene that codes for a protein homologous to human adrenodoxin."
    Barros M.H., Nobrega F.G.
    Gene 233:197-203(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: IDENTIFICATION, SUBCELLULAR LOCATION.
• iron-sulfur cluster binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm for iron-sulfur cluster assembly and tRNA thiolation in yeast."
    Pandey A.K., Pain J., Dancis A., Pain D.
    J. Biol. Chem. 294:9489-9502(2019) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae."
    Barros M.H., Nobrega F.G., Tzagoloff A.
    J Biol Chem 277:9997-10002(2002) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• heme A biosynthetic process Source: SGDInferred from mutant phenotypeⁱ
  • "Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae."
    Barros M.H., Nobrega F.G., Tzagoloff A.
    J Biol Chem 277:9997-10002(2002) [PubMed] [Europe PMC] [Abstract]
• iron-sulfur cluster assembly Source: UniProtKBInferred from direct assayⁱ
  • Ref.4

    "A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins."
    Lange H., Kaut A., Kispal G., Lill R.
    Proc. Natl. Acad. Sci. U.S.A. 97:1050-1055(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• ubiquinone biosynthetic process Source: SGDInferred from mutant phenotypeⁱ
  • "Involvement of mitochondrial ferredoxin and para-aminobenzoic acid in yeast coenzyme Q biosynthesis."
    Pierrel F., Hamelin O., Douki T., Kieffer-Jaquinod S., Muhlenhoff U., Ozeir M., Lill R., Fontecave M.
    Chem Biol 17:449-459(2010) [PubMed] [Europe PMC] [Abstract]
  • "Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency."
    Ozeir M., Muhlenhoff U., Webert H., Lill R., Fontecave M., Pierrel F.
    Chem. Biol. 18:1134-1142(2011) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MLKIVTRAGH TARISNIAAH LLRTSPSLLT RTTTTTRFLP FSTSSFLNHG 
        60         70         80         90        100
HLKKPKPGEE LKITFILKDG SQKTYEVCEG ETILDIAQGH NLDMEGACGG 
       110        120        130        140        150
SCACSTCHVI VDPDYYDALP EPEDDENDML DLAYGLTETS RLGCQIKMSK 
       160        170 
DIDGIRVALP QMTRNVNNND FS                               

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome XVI
   Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families