A0AAD5BM78 · A0AAD5BM78_AMBAR

Function

function

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Mo-molybdopterin (UniProtKB | Rhea| CHEBI:71302 )

Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

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

Note: Binds 2 [2Fe-2S] clusters.

Pathway

Alkaloid biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site52[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site57[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site60[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site82[2Fe-2S] cluster 1 (UniProtKB | ChEBI)
Binding site122[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site125[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site158[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site160[2Fe-2S] cluster 2 (UniProtKB | ChEBI)
Binding site287-294FAD (UniProtKB | ChEBI)
Binding site367FAD (UniProtKB | ChEBI)
Binding site377-381FAD (UniProtKB | ChEBI)
Binding site390FAD (UniProtKB | ChEBI)
Binding site434FAD (UniProtKB | ChEBI)
Binding site452FAD (UniProtKB | ChEBI)
Binding site798Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Binding site829Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Binding site833substrate
Binding site911substrate
Binding site943Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)
Binding site945substrate
Binding site1041substrate
Binding site1110Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular FunctionFAD binding
Molecular Functioniron ion binding
Molecular Functionoxidoreductase activity
Biological Processalkaloid metabolic process
Biological Processferredoxin metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    xanthine dehydrogenase
  • EC number

Gene names

    • ORF names
      M8C21_013218

Organism names

  • Taxonomic identifier
  • Strain
    • AA19_3_7
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Asteroideae > Heliantheae alliance > Heliantheae > Ambrosia

Accessions

  • Primary accession
    A0AAD5BM78

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain14-1002Fe-2S ferredoxin-type
Domain259-444FAD-binding PCMH-type

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,304
  • Mass (Da)
    143,658
  • Last updated
    2024-05-29 v1
  • Checksum
    63A323EC35750FC8
MGSLKTEEDIEESKDAILYVNGIRTVLPDGLAHLTLLEYLRDAGLTGTKLGCGEGGCGACTVMVSYFDQNSKKCVHQAINACLAPLYSVEGMHVITVEGVGNRKFGLHPVQESLASRHGSQCGFCTPGFIMSMYALLRSSKTPPTEEQIEESLAGNLCRCTGYRPILDAFRVFAKSNDLLYTSGSVSVHEPKNGEFICPSTGKPCSCGPNKETVEPSDACQNGYKPVSYNDVDGSSYTNKEIIFPPQLLTRKSSSLSLTGFGGIKWHRPLLLKHVLELKSRHPDAKLVVGNTELGIETRLKKIHYPVFISVTHVPELNILTVGNDGMEIGAGVRLSELQKFLKKVIEERPAYETSSCKAIIEQIKWFAGTQIRNVASVGGNICTASPISDLNPLWMASRAKFKVVDSKGSIRTILAENFFLGYRKVDLGNNEILLSVLLPWTREFEYVKEFKQAHRRDDDIALVNGGMRVFIEKSNKKWIVSDACVVYGGVAPVSLSAVKTKDYLIGKAWDKELLQNSLEILKQDVVISEDAPGGMVEFRKSLTLSFFFKFFLWVSHQMNGQEFFNESVPASHLSAVESFHRPSVMGSQDYEITKQGTAVGSPEVHMSARLQVTGEAEYTDDTPMPPGGLHAALILSKKPHARLLSIDDSGARSSPGFAGIFFNKDIPGSKFTGPIIEDEEVFASEIVTCVGQVIGVAVADTLENAKLAARKVVIEYEDLPAILSIEDAVEFKSFHPNTHRCLSKGDVDLCFQSDQCHKIIEGEVHIGGQEHFYLEPQSTFVWTMDGGHEVHMISSTQAPQKHQKYVAHVLGLPMSKVVCKVKRIGGGFGGKETRSAFIAAVASVPAYLLNRPVKLTLDRDIDMQLTGQRHSFLAKYKVGFTNEGKVLALDLEIYNNAGNSLDLSLAILDRSMYHSDNVYEIPNVRINGSVCFTNYPSNTAFRGFGGPQGMLVSENWIQRIAVEVKKSPEEIREINFNSEGSILHYGQQLQDCTLHRLWDELKKSCNFVKVRSEVDDFNLHNRWKKRGVAMIPTKFGISFTTKFMNQAGALVQVYTDGTVLVTHGGVEMGQGLHTKVAQIAASAFEIPLSSVFISETSTDKVPNASPTAASASSDMYGAAVLDACKQIKARMEPIASLKKHTSFVELVNACYFERIDLSAHGFHVVPDIGFDWKTGKGHPFRYFTYGAAFAEVEIDTLTGDFHTRAADVILDLGFSINPAIDVGQIEGAFIQGMGWVALEELKWGDAAHKWIPPGCLFTSGPGNYKIPSVNDVPFKFKVSLLKLNLFLRSVQPIYNDFDRKEET

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAMZMK010011818
EMBL· GenBank· DDBJ
KAI7725930.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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