Ferric reductase transmembrane component 3 (Q08905)

Identification
NameFerric reductase transmembrane component 3
Synonyms
  • Ferric-chelate reductase 3
Gene NameFRE3
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionSiderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to di- and trihydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane
Cellular LocationCell 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
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
FAD or FADH2 binding
ion binding
cation binding
metal ion binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
electron carrier activity
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 15
LocusYOR381W
Gene Sequence>2136 bp ATGTATTGGGTCCTCCTTTGTGGTTCTATTTTGTTATGCTGCTTGTCAGGAGCAAGCGCC TCCCCTGCTAAGACAAAAATGTACGGCAAGTTACCACTGGTTTTGACAGATGCCTGCATG GGAGTTCTCGGCGAAGTAACCTGGGAGTATAGTAGTGACGATTTATATTCCTCACCAGCA TGTACATATGAACCGGCATTACAGTCAATGTTGTATTGTATTTACGAATCATTGAATGAA AAGGGTTATTCCAATAGAACCTTTGAAAAAACCTTTGCTGCTATCAAAGAAGACTGCGCA TATTACACTGATAACCTTCAGAATATGACTAATGCAGATTTCTATAATATGCTGAATAAT GGAACAACATACATAATACAGTATTCTGAAGGTAGCGCGAATCTTACGTATCCAATCGAG ATGGATGCCCAAGTGAGAGAAAACTATTATTATTCTTACCATGGTTTCTACGCCAACTAC GACATTGGTCATACTTATGGTGGTATTATTTGCGCCTATTTTGTAGGTGTTATGATTCTT GCCAGCATACTCCATTATCTAAGTTACACTCCGTTTAAAACTGCCTTATTTAAACAAAGA CTTGTAAGATATGTGAGAAGATATTTGACAATACCTACTATCTGGGGTAAACATGCGTCG AGCTTTTCTTACCTTAAAATTTTTACAGGCTTCCTTCCCACACGATCTGAAGGCGTCATT ATACTTGGATACCTCGTGCTTCATACAGTTTTTCTGGCATACGGGTATCAATATGATCCT TACAACTTAATTTTCGACTCTCGTAGAGAACAGATTGCTCGATACGTGGCAGATAGAAGT GGTGTCCTGGCATTTGCACATTTTCCCCTAATAGCTCTTTTCGCAGGAAGGAACAATTTT CTAGAATTCATTTCTGGAGTAAAATATACCTCTTTCATAATGTTTCATAAGTGGTTGGGA AGAATGATGTTTTTAGATGCTGTGATTCATGGCGCTGCTTATACCAGTTATTCCGTATTC TACAAAGATTGGGCAGCAAGCAAGGAAGAGACATATTGGCAATTTGGAGTAGCTGCTCTT TGTATAGTTGGTGTTATGGTGTTTTTTTCTTTGGCAATGTTCAGAAAGTTTTTCTATGAA GCCTTCTTATTTCTCCATATTGTGCTTGGCGCATTGTTCTTTTATACGTGTTGGGAGCAC GTCGTAGAATTGAGTGGGATTGAGTGGATATACGCTGCTATTGCTATCTGGACTATTGAT AGGCTAATTCGAATTGTTAGAGTATCTTATTTCGGTTTCCCTAAGGCTTCCTTACAGTTA GTTGGCGATGACATCATTCGAGTCACAGTCAAACGACCAGTAAGGCTATGGAAAGCCAAA CCAGGACAGTATGTTTTCGTTTCATTCCTACACCACCTGTATTTTTGGCAGTCACATCCT TTCACAGTCTTAGATTCAATTATCAAAGATGGTGAGCTGACTATTATCCTGAAGGAAAAA AAGGGAGTAACAAAACTTGTCAAAAAGTATGTGTGTTGCAATGGAGGTAAGGCATCTATG AGACTAGCTATAGAAGGTCCATATGGCTCTTCATCTCCAGTCAATAATTATGATAACGTC TTGCTACTTACGGGAGGTACTGGTTTGCCAGGGCCCATTGCACACGCCATTAAACTTGGA AAAACGTCAGCGGCAACTGGAAAACAATTCATAAAATTAGTGATTGCAGTTAGAGGGTTT AACGTACTCGAGGCTTACAAGCCGGAGCTGATGTGTCTAGAAGATCTTAATGTACAGCTT CACATCTACAATACAATGGAAGTTCCGGCATTAACTCCTAATGATAGTTTGGAAATTTCT CAACAAGACGAGAAGGCCGATGGAAAAGGTGTTGTTATGGCAACTACCCTAGAACAGTCA CCTAATCCAGTTGAATTTGATGGTACTGTTTTTCATCATGGAAGACCCAATGTTGAAAAG CTTCTGCATGAAGTTGGTGACCTAAATGGATCGTTAGCTGTGGTTTGTTGTGGGCCTCCT GTTTTCGTTGACGAAGTAAGGGATCAAACGGCAAATCTTGTTCTAGAGAAGCCTGCAAAG GCAATCGAATACTTTGAAGAATACCAAAGTTGGTAA
Protein Properties
Pfam Domain Function
Protein Residues711
Protein Molecular Weight80588.5
Protein Theoretical pI7.1
Signalling Regions
  • 1-20
Transmembrane Regions
  • 167-187
  • 238-258
  • 281-301
  • 322-341
  • 354-374
  • 377-397
  • 399-419
Protein Sequence>Ferric reductase transmembrane component 3 MYWVLLCGSILLCCLSGASASPAKTKMYGKLPLVLTDACMGVLGEVTWEYSSDDLYSSPA CTYEPALQSMLYCIYESLNEKGYSNRTFEKTFAAIKEDCAYYTDNLQNMTNADFYNMLNN GTTYIIQYSEGSANLTYPIEMDAQVRENYYYSYHGFYANYDIGHTYGGIICAYFVGVMIL ASILHYLSYTPFKTALFKQRLVRYVRRYLTIPTIWGKHASSFSYLKIFTGFLPTRSEGVI ILGYLVLHTVFLAYGYQYDPYNLIFDSRREQIARYVADRSGVLAFAHFPLIALFAGRNNF LEFISGVKYTSFIMFHKWLGRMMFLDAVIHGAAYTSYSVFYKDWAASKEETYWQFGVAAL CIVGVMVFFSLAMFRKFFYEAFLFLHIVLGALFFYTCWEHVVELSGIEWIYAAIAIWTID RLIRIVRVSYFGFPKASLQLVGDDIIRVTVKRPVRLWKAKPGQYVFVSFLHHLYFWQSHP FTVLDSIIKDGELTIILKEKKGVTKLVKKYVCCNGGKASMRLAIEGPYGSSSPVNNYDNV LLLTGGTGLPGPIAHAIKLGKTSAATGKQFIKLVIAVRGFNVLEAYKPELMCLEDLNVQL HIYNTMEVPALTPNDSLEISQQDEKADGKGVVMATTLEQSPNPVEFDGTVFHHGRPNVEK LLHEVGDLNGSLAVVCCGPPVFVDEVRDQTANLVLEKPAKAIEYFEEYQSW
References
External Links
ResourceLink
Saccharomyces Genome Database FRE3
Uniprot IDQ08905
Uniprot NameFRE3_YEAST
GenBank Gene IDZ75289
Genebank Protein ID1420821
General Reference
  • 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, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • 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
  • Yun, C. W., Bauler, M., Moore, R. E., Klebba, P. E., Philpott, C. C. (2001). "The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae." J Biol Chem 276:10218-10223.11120744
  • 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