Q12184 · ADRX_YEAST

Function

function

Iron-sulfur protein that transfers electrons in a wide variety of metabolic reactions. Involved in heme A biosynthesis and in iron-sulfur cluster assembly (PubMed:10655482).
Transfers electrons from adrenodoxin reductase ARH1 to heme A synthase COX15, a heme protein that catalyzes the conversion of heme O to heme A (PubMed:11248251, PubMed:11788607).
Required for the de novo synthesis of Fe-S clusters on iron sulfur cluster assembly protein ISU1. Interact in its reduced state with ISU1 to productively deliver electrons for Fe-S cluster synthesis (PubMed:12970193, PubMed:15211518, PubMed:25358379).
Essential for coenzyme Q biosynthesis. May transfer the electrons required for the hydroxylation reaction performed by COQ6 (PubMed:20534343, PubMed:21944752).

Miscellaneous

Present with 14800 molecules/cell in log phase SD medium.

Cofactor

[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster.

Features

Showing features for binding site.

117220406080100120140160
TypeIDPosition(s)Description
Binding site98[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site104[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site107[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site144[2Fe-2S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentiron-sulfur cluster assembly complex
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular Functioniron-sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on NAD(P)H, heme protein as acceptor
Biological Processelectron transport chain
Biological Processheme A biosynthetic process
Biological Processiron-sulfur cluster assembly
Biological ProcessP450-containing electron transport chain
Biological Processubiquinone biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Adrenodoxin homolog, mitochondrial
  • Alternative names
    • Mitochondrial ferredoxin

Gene names

    • Name
      YAH1
    • Ordered locus names
      YPL252C

Organism names

Accessions

  • Primary accession
    Q12184
  • Secondary accessions
    • D6W3B9

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-16Mitochondrion
ChainPRO_000000099417-172Adrenodoxin homolog, mitochondrial

Proteomic databases

Interaction

Subunit

Interacts in its reduced state with the apo form of ISU1.
View interactors in UniProtKB
View CPX-392 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain61-1632Fe-2S ferredoxin-type

Sequence similarities

Belongs to the adrenodoxin/putidaredoxin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    172
  • Mass (Da)
    18,932
  • Last updated
    1996-11-01 v1
  • Checksum
    D7DB9CFACBED1BFC
MLKIVTRAGHTARISNIAAHLLRTSPSLLTRTTTTTRFLPFSTSSFLNHGHLKKPKPGEELKITFILKDGSQKTYEVCEGETILDIAQGHNLDMEGACGGSCACSTCHVIVDPDYYDALPEPEDDENDMLDLAYGLTETSRLGCQIKMSKDIDGIRVALPQMTRNVNNNDFS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z73608
EMBL· GenBank· DDBJ
CAA97975.1
EMBL· GenBank· DDBJ
Genomic DNA
Z67751
EMBL· GenBank· DDBJ
CAA91592.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006949
EMBL· GenBank· DDBJ
DAA11185.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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