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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)DescriptionActionsGraphical viewLength
Metal bindingi310Iron (heme 1 axial ligand)By similarity1
Metal bindingi324Iron (heme 2 axial ligand)By similarity1
Metal bindingi380Iron (heme 1 axial ligand)By similarity1
Metal bindingi394Iron (heme 2 axial ligand)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi473 – 479FADSequence analysis7
Nucleotide bindingi520 – 523NADPSequence analysis4
Nucleotide bindingi660 – 661NADPSequence analysis2

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)DescriptionActionsGraphical viewLength
Topological domaini20 – 163ExtracellularBy similarityAdd BLAST144
Transmembranei164 – 184Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini185 – 222CytoplasmicBy similarityAdd BLAST38
Transmembranei223 – 243Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini244 – 267ExtracellularBy similarityAdd BLAST24
Transmembranei268 – 288Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini289 – 311CytoplasmicBy similarityAdd BLAST23
Transmembranei312 – 334Helical; Name=4Sequence analysisAdd BLAST23
Topological domaini335 – 347ExtracellularBy similarityAdd BLAST13
Transmembranei348 – 368Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini369 – 371CytoplasmicBy similarity3
Transmembranei372 – 392Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini393 – 403ExtracellularBy similarityAdd BLAST11
Transmembranei404 – 424Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini425 – 694CytoplasmicBy similarityAdd BLAST270

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001014120 – 694Ferric reductase transmembrane component 5Add BLAST675

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ08908.

Expressioni

Inductioni

By iron deprivation.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi34765. 3 interactors.
DIPiDIP-2747N.
IntActiQ08908. 1 interactor.
MINTiMINT-1590821.

Structurei

3D structure databases

ProteinModelPortaliQ08908.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini274 – 408Ferric oxidoreductaseAdd BLAST135
Domaini409 – 528FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST120

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi362 – 368Poly-Phe7

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.
OrthoDBiEOG092C04QA.

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 interactors.
DIPiDIP-2747N.
IntActiQ08908. 1 interactor.
MINTiMINT-1590821.

Proteomic databases

PRIDEiQ08908.

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.
OrthoDBiEOG092C04QA.

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...

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: November 2, 2016
This is version 134 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.