Q04800 · FRP1_SCHPO
- ProteinFerric reductase transmembrane component 1
- Genefrp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids564 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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
- 2 a Fe(II)-siderophore + H+ + NADP+ = 2 a Fe(III)-siderophore + NADPH
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 157 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 171 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 225 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 239 | Fe (UniProtKB | ChEBI) of heme 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 317-323 | FAD (UniProtKB | ChEBI) | ||||
Sequence: HPFTIAS | ||||||
Binding site | 419-427 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: LFAGGVGVS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ferric-chelate reductase (NADPH) activity | |
Molecular Function | ferric-chelate reductase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | iron ion binding | |
Biological Process | cellular response to iron ion starvation | |
Biological Process | copper ion transmembrane transport | |
Biological Process | reductive iron assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFerric reductase transmembrane component 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionQ04800
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 10-30 | Helical | ||||
Sequence: TVIAICLILGILLAFILMFWL | ||||||
Transmembrane | 73-93 | Helical | ||||
Sequence: VILTLIAVPVVFAISIPFIGM | ||||||
Transmembrane | 117-137 | Helical | ||||
Sequence: VAARLGFLACGLYVTSYFFSI | ||||||
Transmembrane | 160-180 | Helical | ||||
Sequence: LSQYAIMIGAIHGFAYIGLAA | ||||||
Transmembrane | 193-213 | Helical | ||||
Sequence: IIGYVILGLMVIMIVSSLPFF | ||||||
Transmembrane | 417-437 | Helical | ||||
Sequence: LFLFAGGVGVSYILPIILDTI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000210152 | 1-564 | Ferric reductase transmembrane component 1 | |||
Sequence: MAINSSDKWTVIAICLILGILLAFILMFWLERFRVIIKSNAHKHDPSDKRQIWLEKYYLFVRQIYTYLVTHKVILTLIAVPVVFAISIPFIGMQTPASSHGKQTTQVSTGNWSKNAVAARLGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVYVFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFTIASVPSDDFIELFVAVRAGFTKRLAKKVSSKSLSDVSDINISDEKIEKNGDVGIEVMERHSLSQEDLVFESSAAKVSVLMDGPYGPVSNPYKDYSYLFLFAGGVGVSYILPIILDTIKKQSRTVHITFVWSARSSALLNIVHKSLCEAVRYTEMNINIFCHLTNSYPVEEVSSLNSQSARNYSLQYLNGRPDVNDYFKDFLHATGTQTAALASCGSDKLLRHLKSCVNTHSPSTVDLYQHYEEI | ||||||
Glycosylation | 4 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 268 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 360 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 362 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 381 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 383 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 501 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 121-254 | Ferric oxidoreductase | ||||
Sequence: LGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVY | ||||||
Domain | 255-410 | FAD-binding FR-type | ||||
Sequence: VFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFTIASVPSDDFIELFVAVRAGFTKRLAKKVSSKSLSDVSDINISDEKIEKNGDVGIEVMERHSLSQEDLVFESSAAKVSVLMDGPYGPVSNP |
Sequence similarities
Belongs to the ferric reductase (FRE) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length564
- Mass (Da)64,092
- Last updated1994-02-01 v1
- Checksum336CC2AF934A736B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L07749 EMBL· GenBank· DDBJ | AAA68045.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CU329671 EMBL· GenBank· DDBJ | CAB91171.1 EMBL· GenBank· DDBJ | Genomic DNA |