FRE5_YEAST
ID FRE5_YEAST Reviewed; 694 AA.
AC Q08908; D6W377;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ferric reductase transmembrane component 5;
DE EC=1.16.1.9;
DE AltName: Full=Ferric-chelate reductase 5;
DE Flags: Precursor;
GN Name=FRE5; OrderedLocusNames=YOR384W; ORFNames=O6765;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INDUCTION.
RX PubMed=9726978; DOI=10.1074/jbc.273.37.23716;
RA Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RT "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:23716-23721(1998).
RN [5]
RP ERRATUM OF PUBMED:9726978.
RA Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R.;
RL J. Biol. Chem. 273:30056-30056(1998).
RN [6]
RP INDUCTION.
RX PubMed=10341420;
RX DOI=10.1002/(sici)1097-0061(199905)15:7<573::aid-yea404>3.0.co;2-7;
RA Georgatsou E., Alexandraki D.;
RT "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu
RT reductase related genes.";
RL Yeast 15:573-584(1999).
CC -!- FUNCTION: Metalloreductase responsible for reducing extracellular iron
CC and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-
CC salts and Fe(3+) bound to catecholate or hydroxamate siderophores.
CC Fe(3+) is reduced to Fe(2+), which then dissociates from the
CC siderophore and can be imported by the high-affinity Fe(2+) transport
CC complex in the plasma membrane (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-
CC siderophore + NADPH; Xref=Rhea:RHEA:28795, Rhea:RHEA-COMP:11342,
CC Rhea:RHEA-COMP:11344, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: By iron deprivation. {ECO:0000269|PubMed:10341420,
CC ECO:0000269|PubMed:9726978}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000305}.
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DR EMBL; Z75292; CAA99716.1; -; Genomic_DNA.
DR EMBL; AY692958; AAT92977.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11143.1; -; Genomic_DNA.
DR PIR; S67296; S67296.
DR RefSeq; NP_015029.1; NM_001183804.1.
DR AlphaFoldDB; Q08908; -.
DR SMR; Q08908; -.
DR BioGRID; 34765; 20.
DR DIP; DIP-2747N; -.
DR IntAct; Q08908; 1.
DR MINT; Q08908; -.
DR STRING; 4932.YOR384W; -.
DR PaxDb; Q08908; -.
DR PRIDE; Q08908; -.
DR EnsemblFungi; YOR384W_mRNA; YOR384W; YOR384W.
DR GeneID; 854566; -.
DR KEGG; sce:YOR384W; -.
DR SGD; S000005911; FRE5.
DR VEuPathDB; FungiDB:YOR384W; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000176662; -.
DR HOGENOM; CLU_010365_4_0_1; -.
DR InParanoid; Q08908; -.
DR OMA; YNEDAHM; -.
DR BioCyc; YEAST:G3O-33846-MON; -.
DR PRO; PR:Q08908; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08908; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; ISA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0015677; P:copper ion import; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Electron transport; FAD; Flavoprotein; Glycoprotein; Heme;
KW Ion transport; Iron; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..694
FT /note="Ferric reductase transmembrane component 5"
FT /id="PRO_0000010141"
FT TOPO_DOM 20..163
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..184
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 223..243
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..267
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 268..288
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..334
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..347
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 348..368
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 372..392
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..403
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 404..424
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..694
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 274..408
FT /note="Ferric oxidoreductase"
FT DOMAIN 409..528
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 310
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 473..479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 520..523
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 660..661
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 694 AA; 80292 MW; 44D7E941F19F7AA0 CRC64;
MLFARLVLLL VYLAPGSLAK PASTKKRTQW DQIAIDACAK ELESHKFDTD VKGRHATLCT
YEPALGSWLH CAKDVLDSRK KSKKIFEKTF SKINQYCHDY HKDEVVSNEE YYRIFANASL
FIRPLDEVKE NIRYPVTPNK ASLDRWVWAY FGPLDNIDKG NVYGVTICLY WIGVLFIAAV
YHFLNFSRLK QTVFKNKVSA FLRGHYVLPA LVHNHAMSVG RWFFIGLVPT RLETLVLFGY
VLLHGFLLSS YNFDHNELLS DRRSQVLIFL SDRAGILAFA HFPLIVLFGG KNSTMTWLTG
IRYTAFITYH KWLGRFMLVD CTIHAIGYTY HAYIENYWKY VKYSDLWTSG RHAMIIVGIL
VFFSFFFFRR HYYELFVITH IILAIGFFHA CWKHCYKLGW GEWIMACALF WIADRILRLI
KIAIFGMPWA KLKLCGESMI EVRISKSSKW WKAEPGQYIY LYFLRPKIFW QSHPFTVMDS
LVEDGELVVV ITVKNGLTKK LQEYLLESEG YTEMRVLAEG PYGQSTRTHL FESLLFIAGG
AGVPGPLSMA IKAGRQVKSN DSHQMIKFVW SVRNLDLLEV YRKEIMVLKE LNIDTKIYFT
GERKDESNTE EGAIANMSTE GRLLTTSKSA EMITDFGRPN IDEIIEEAVS GAKSLLVTCC
GSEGFVDKTR ELTAKRVLEH GDKWIEYVEE FQNW
