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Protein

Ferric reductase transmembrane component 5

Gene

FRE5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe3+-salts and Fe3+ bound to catecholate or hydroxamate siderophores. 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).By similarity

Catalytic activityi

2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH.

Cofactori

FADCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi310 – 3101Iron (heme 1 axial ligand)By similarity
Metal bindingi324 – 3241Iron (heme 2 axial ligand)By similarity
Metal bindingi380 – 3801Iron (heme 1 axial ligand)By similarity
Metal bindingi394 – 3941Iron (heme 2 axial ligand)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi473 – 4797FADSequence analysis
Nucleotide bindingi520 – 5234NADPSequence analysis
Nucleotide bindingi660 – 6612NADPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Ion transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciYEAST:G3O-33846-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferric reductase transmembrane component 5 (EC:1.16.1.9)
Alternative name(s):
Ferric-chelate reductase 5
Gene namesi
Name:FRE5
Ordered Locus Names:YOR384W
ORF Names:O6765
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR384W.
SGDiS000005911. FRE5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 163144ExtracellularBy similarityAdd
BLAST
Transmembranei164 – 18421Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini185 – 22238CytoplasmicBy similarityAdd
BLAST
Transmembranei223 – 24321Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini244 – 26724ExtracellularBy similarityAdd
BLAST
Transmembranei268 – 28821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini289 – 31123CytoplasmicBy similarityAdd
BLAST
Transmembranei312 – 33423Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini335 – 34713ExtracellularBy similarityAdd
BLAST
Transmembranei348 – 36821Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini369 – 3713CytoplasmicBy similarity
Transmembranei372 – 39221Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini393 – 40311ExtracellularBy similarityAdd
BLAST
Transmembranei404 – 42421Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini425 – 694270CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 694675Ferric reductase transmembrane component 5PRO_0000010141Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

By iron deprivation.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi34765. 3 interactions.
DIPiDIP-2747N.
IntActiQ08908. 1 interaction.
MINTiMINT-1590821.

Structurei

3D structure databases

ProteinModelPortaliQ08908.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini274 – 408135Ferric oxidoreductaseAdd
BLAST
Domaini409 – 528120FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi362 – 3687Poly-Phe

Sequence similaritiesi

Belongs to the ferric reductase (FRE) family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000000805.
InParanoidiQ08908.
KOiK00521.
OMAiIGYTYHA.
OrthoDBiEOG7PGF10.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFARLVLLL VYLAPGSLAK PASTKKRTQW DQIAIDACAK ELESHKFDTD
60 70 80 90 100
VKGRHATLCT YEPALGSWLH CAKDVLDSRK KSKKIFEKTF SKINQYCHDY
110 120 130 140 150
HKDEVVSNEE YYRIFANASL FIRPLDEVKE NIRYPVTPNK ASLDRWVWAY
160 170 180 190 200
FGPLDNIDKG NVYGVTICLY WIGVLFIAAV YHFLNFSRLK QTVFKNKVSA
210 220 230 240 250
FLRGHYVLPA LVHNHAMSVG RWFFIGLVPT RLETLVLFGY VLLHGFLLSS
260 270 280 290 300
YNFDHNELLS DRRSQVLIFL SDRAGILAFA HFPLIVLFGG KNSTMTWLTG
310 320 330 340 350
IRYTAFITYH KWLGRFMLVD CTIHAIGYTY HAYIENYWKY VKYSDLWTSG
360 370 380 390 400
RHAMIIVGIL VFFSFFFFRR HYYELFVITH IILAIGFFHA CWKHCYKLGW
410 420 430 440 450
GEWIMACALF WIADRILRLI KIAIFGMPWA KLKLCGESMI EVRISKSSKW
460 470 480 490 500
WKAEPGQYIY LYFLRPKIFW QSHPFTVMDS LVEDGELVVV ITVKNGLTKK
510 520 530 540 550
LQEYLLESEG YTEMRVLAEG PYGQSTRTHL FESLLFIAGG AGVPGPLSMA
560 570 580 590 600
IKAGRQVKSN DSHQMIKFVW SVRNLDLLEV YRKEIMVLKE LNIDTKIYFT
610 620 630 640 650
GERKDESNTE EGAIANMSTE GRLLTTSKSA EMITDFGRPN IDEIIEEAVS
660 670 680 690
GAKSLLVTCC GSEGFVDKTR ELTAKRVLEH GDKWIEYVEE FQNW
Length:694
Mass (Da):80,292
Last modified:November 1, 1996 - v1
Checksum:i44D7E941F19F7AA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75292 Genomic DNA. Translation: CAA99716.1.
AY692958 Genomic DNA. Translation: AAT92977.1.
BK006948 Genomic DNA. Translation: DAA11143.1.
PIRiS67296.
RefSeqiNP_015029.1. NM_001183804.1.

Genome annotation databases

EnsemblFungiiYOR384W; YOR384W; YOR384W.
GeneIDi854566.
KEGGisce:YOR384W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75292 Genomic DNA. Translation: CAA99716.1.
AY692958 Genomic DNA. Translation: AAT92977.1.
BK006948 Genomic DNA. Translation: DAA11143.1.
PIRiS67296.
RefSeqiNP_015029.1. NM_001183804.1.

3D structure databases

ProteinModelPortaliQ08908.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34765. 3 interactions.
DIPiDIP-2747N.
IntActiQ08908. 1 interaction.
MINTiMINT-1590821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR384W; YOR384W; YOR384W.
GeneIDi854566.
KEGGisce:YOR384W.

Organism-specific databases

EuPathDBiFungiDB:YOR384W.
SGDiS000005911. FRE5.

Phylogenomic databases

GeneTreeiENSGT00390000007891.
HOGENOMiHOG000000805.
InParanoidiQ08908.
KOiK00521.
OMAiIGYTYHA.
OrthoDBiEOG7PGF10.

Enzyme and pathway databases

BioCyciYEAST:G3O-33846-MONOMER.

Miscellaneous databases

PROiQ08908.

Family and domain databases

InterProiIPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae."
    Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
    J. Biol. Chem. 273:23716-23721(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Erratum
    Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.
    J. Biol. Chem. 273:30056-30056(1998)
  6. "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes."
    Georgatsou E., Alexandraki D.
    Yeast 15:573-584(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiFRE5_YEAST
AccessioniPrimary (citable) accession number: Q08908
Secondary accession number(s): D6W377
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.