Q04800 · FRP1_SCHPO

Function

function

Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity).
Catalyzes the reductive uptake of Fe3+-salts and Fe3+ bound to catecholate or hydroxamate siderophores (By similarity).
Fe3+ is reduced to Fe2+, which then dissociates from the siderophore and can be imported by the high-affinity Fe2+ transport complex in the plasma membrane (By similarity).
Also participates in Cu2+ reduction and Cu+ uptake (By similarity).

Catalytic activity

Cofactor

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

heme (UniProtKB | Rhea| CHEBI:30413 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site157Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue
Binding site171Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue
Binding site225Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue
Binding site239Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue
Binding site317-323FAD (UniProtKB | ChEBI)
Binding site419-427NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionferric-chelate reductase (NADPH) activity
Molecular Functionferric-chelate reductase activity
Molecular Functionflavin adenine dinucleotide binding
Molecular Functioniron ion binding
Biological Processcellular response to iron ion starvation
Biological Processcopper ion transmembrane transport
Biological Processreductive iron assimilation

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Ferric reductase transmembrane component 1
  • EC number
  • Alternative names
    • Ferric-chelate reductase 1

Gene names

    • Name
      frp1
    • ORF names
      SPBC1683.09c

Organism names

Accessions

  • Primary accession
    Q04800

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane10-30Helical
Transmembrane73-93Helical
Transmembrane117-137Helical
Transmembrane160-180Helical
Transmembrane193-213Helical
Transmembrane417-437Helical

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002101521-564Ferric reductase transmembrane component 1
Glycosylation4N-linked (GlcNAc...) asparagine
Glycosylation111N-linked (GlcNAc...) asparagine
Glycosylation268N-linked (GlcNAc...) asparagine
Glycosylation360N-linked (GlcNAc...) asparagine
Modified residue362Phosphoserine
Modified residue381Phosphoserine
Modified residue383Phosphoserine
Glycosylation501N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain121-254Ferric oxidoreductase
Domain255-410FAD-binding FR-type

Sequence similarities

Belongs to the ferric reductase (FRE) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    564
  • Mass (Da)
    64,092
  • Last updated
    1994-02-01 v1
  • Checksum
    336CC2AF934A736B
MAINSSDKWTVIAICLILGILLAFILMFWLERFRVIIKSNAHKHDPSDKRQIWLEKYYLFVRQIYTYLVTHKVILTLIAVPVVFAISIPFIGMQTPASSHGKQTTQVSTGNWSKNAVAARLGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVYVFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFTIASVPSDDFIELFVAVRAGFTKRLAKKVSSKSLSDVSDINISDEKIEKNGDVGIEVMERHSLSQEDLVFESSAAKVSVLMDGPYGPVSNPYKDYSYLFLFAGGVGVSYILPIILDTIKKQSRTVHITFVWSARSSALLNIVHKSLCEAVRYTEMNINIFCHLTNSYPVEEVSSLNSQSARNYSLQYLNGRPDVNDYFKDFLHATGTQTAALASCGSDKLLRHLKSCVNTHSPSTVDLYQHYEEI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L07749
EMBL· GenBank· DDBJ
AAA68045.1
EMBL· GenBank· DDBJ
Genomic DNA
CU329671
EMBL· GenBank· DDBJ
CAB91171.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp