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Identification
NameFerric reductase transmembrane component 6
Synonyms
  • Ferric-chelate reductase 6
Gene NameFRE6
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionMetalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe(3+) to Fe(2+) and Cu(2+) to Cu(+), respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol
Cellular LocationVacuole membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00194Iron(3+)Show
YMDB00379Iron(2+)Show
YMDB00426NADPHShow
YMDB00427NADPShow
GO Classification
Component
membrane part
intrinsic to membrane
integral to membrane
cell part
Function
transition metal ion binding
iron ion binding
oxidoreductase activity
binding
nucleoside binding
electron carrier activity
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
catalytic activity
ion binding
cation binding
metal ion binding
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 12
LocusYLL051C
Gene Sequence>2139 bp ATGCATAGAACGCTTCTGTTTTTAACGTGGCTGATATCTTTAACAAAGGCTTTTAATATA AAATTACCACACACTGAAAAAAAAGACCATTTGGAATCCAACGCTGTGCTGGCATGCGCA TCCTATATAAATACTCTGAAGTGGTCATTTGATAGCTCCGTCGTACCGGGTTTCTATTCT ACCATATGCTCTTATTCACCAGCGTTTGATACTTGGTCACTTTGTATCTTCAATTCGCTT ACAGACCAGATTATTCCCATGGACAACACAAGTTTCGAAGAAAGCTTGGGTAACGTACGA AAAACGTGCTCGTTTGTCGATAAAAAGTTTAGCAATATTTCACTGGAGCAATACTACTCA TCTTTAAATAATGCTTCTTCTCACGCTTTGGAAGACTATGGTTCTATTGAAAGTTTATCG ACATCCATTCGAGTCGATCGTGAGACAAGATCTAGATGGATACGAGCTTTTCATGCGCAT GCCTATAATTTAGATATCAGCAGTGTTTATGGTGCATATTTAACTTACTACTTCGTCATA GTGGGTATTATCGCCGTCTTCTTCCATATGAGTCACTATAACGGCCTGAATCGAGCGCTA TTTGCAAGCCGGTTCGTCAATTATATTCGGGGCCATTTTGTGTTGCCTACGTTTTTAGTA GATAAGCACGCTAATCACTTCAAGTTTCTAAACGTGGAAGTCTTTACGGGACTGATGCCG AATTCCTTGGAGGCATGGATCATTTTTGGATACACATTGGCGAACATCATATTTTTGTCC ATAAGTTACATCATAGACCCATATAACCTCATTTTCAACAGTCACCTGTCGCAGTTTACA AGACTGTTGGCTGATAGATCTGGGATACTGGCGTTTACTCAGTTCCCTCTCATTATCATT TTTACGGCAAGGAATAGTTTTCTCGAATTTTTAACAGGAGTCAAGTTCAATTCCTTTATT AGTTTCCATAAATGGATCGGTAGAATCATGGTCTTAAACGCAACGATACATTCGCTTTCT TATTCATTATTCGCAATTATCAACCATGCCTTCAAAATAAGCAACAAACAGCTCTATTGG AAGTTTGGTATTGCATCCATAACAGTGCTTTGCGTTCTACTAGTTCTATCGCTCGGAATA GTAAGGAAAAGACATTACGAATTTTTCCTGTACACCCACATCATACTAGCCCTTTTGTTC TTTTACTGTTGTTGGCAACACGTCAAAATTTTCAACGGTTGGAAAGAATGGATAGTGGTA TCCTTGCTCATTTGGGGGCTGGAAAAGCTTTTCAGAATATGGAACATTTTGCAGTTTAGA TTTCCGAAAGCAACACTAATCAATTTGAACACCAGCAACAACCCGCACGATGAAATGTTT AAAGTAATCATACCCAAATATAACCGGAGATGGCATTCGAAACCGGGTCAATATTGTTTC ATTTATTTTTTACATCCATTGGTATTTTGGCAATGCCATCCATTTACCATTATCGACGAA GGTGAGAAGTGTGTTTTAGTGATCAAACCTAAAAGTGGTCTCACTAGATTCATTTATAAC CATATTTTGCAATCTTTAAATGGTAAATTACAACTCCGAGTGGCCATTGAGGGACCTTAT GGGCCCAGTAATCTTCACCTCGATAAATTCGACCATTTGCTGTTACTAAGTGGAGGAACA GGCTTGCCTGGTCCATTAGATCATGCCATTAAGCTGTCACGAAACCCTGATAAACCCAAG AGTATAGATTTGATCATGGCGATCAAAAATCCTTCTTTTCTTAACGGCTATAAATCCGAG ATACTAGAGCTAAAAAATAGCCGATCCCACGTCAACGTGCAGGTTTACCTTACACAGAAA ACAGCTGTTACAAAGGCAGCAAACGCACGAGACCAATTAATACATTTTGATGATATAATG ACCGAACTGACAAGCTTCGCCCACATCGGCAATGCAAGACCTAATTTTAGCAATGTAATT GAAAACGCAATAAAAAGTACGCCGCCTGGAGATTCATTAGCGGTCGTGTGCTGCGGCCCT CCTGTTCTGGTGGACGATGTTAGAAACACCGTTTCTCAAAAACTCCTCGGTTACCCAGAG AGAATTATAGAGTATTTCGAGGAATATCAGTGTTGGTAA
Protein Properties
Pfam Domain Function
Protein Residues712
Protein Molecular Weight81988.29688
Protein Theoretical pI9.13
Signalling Regions
  • 1-17
Transmembrane Regions
  • 168-188
  • 245-265
  • 288-308
  • 329-349
  • 361-381
  • 388-408
  • 417-437
Protein Sequence>Ferric reductase transmembrane component 6 MHRTLLFLTWLISLTKAFNIKLPHTEKKDHLESNAVLACASYINTLKWSFDSSVVPGFYS TICSYSPAFDTWSLCIFNSLTDQIIPMDNTSFEESLGNVRKTCSFVDKKFSNISLEQYYS SLNNASSHALEDYGSIESLSTSIRVDRETRSRWIRAFHAHAYNLDISSVYGAYLTYYFVI VGIIAVFFHMSHYNGLNRALFASRFVNYIRGHFVLPTFLVDKHANHFKFLNVEVFTGLMP NSLEAWIIFGYTLANIIFLSISYIIDPYNLIFNSHLSQFTRLLADRSGILAFTQFPLIII FTARNSFLEFLTGVKFNSFISFHKWIGRIMVLNATIHSLSYSLFAIINHAFKISNKQLYW KFGIASITVLCVLLVLSLGIVRKRHYEFFLYTHIILALLFFYCCWQHVKIFNGWKEWIVV SLLIWGLEKLFRIWNILQFRFPKATLINLNTSNNPHDEMFKVIIPKYNRRWHSKPGQYCF IYFLHPLVFWQCHPFTIIDEGEKCVLVIKPKSGLTRFIYNHILQSLNGKLQLRVAIEGPY GPSNLHLDKFDHLLLLSGGTGLPGPLDHAIKLSRNPDKPKSIDLIMAIKNPSFLNGYKSE ILELKNSRSHVNVQVYLTQKTAVTKAANARDQLIHFDDIMTELTSFAHIGNARPNFSNVI ENAIKSTPPGDSLAVVCCGPPVLVDDVRNTVSQKLLGYPERIIEYFEEYQCW
References
External Links
ResourceLink
Saccharomyces Genome Database FRE6
Uniprot IDQ12473
Uniprot NameFRE6_YEAST
GenBank Gene IDZ47973
Genebank Protein ID642333
General Reference
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Martins, L. J., Jensen, L. T., Simon, J. R., Keller, G. L., Winge, D. R. (1998). "Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae." J Biol Chem 273:23716-23721.9726978
  • Georgatsou, E., Alexandraki, D. (1999). "Regulated expression of the Saccharomyces cerevisiae Fre1p/Fre2p Fe/Cu reductase related genes." Yeast 15:573-584.10341420
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Courel, M., Lallet, S., Camadro, J. M., Blaiseau, P. L. (2005). "Direct activation of genes involved in intracellular iron use by the yeast iron-responsive transcription factor Aft2 without its paralog Aft1." Mol Cell Biol 25:6760-6771.16024809
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258
  • Rees, E. M., Thiele, D. J. (2007). "Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization." J Biol Chem 282:21629-21638.17553781
  • Singh, A., Kaur, N., Kosman, D. J. (2007). "The metalloreductase Fre6p in Fe-efflux from the yeast vacuole." J Biol Chem 282:28619-28626.17681937