NAD(P)H-dependent FMN reductase LOT6 (Q07923)

Identification
NameNAD(P)H-dependent FMN reductase LOT6
Synonyms
  • FMN reductase LOT6
  • Azoreductase LOT6
  • Low temperature response protein 6
Gene NameLOT6
Enzyme Class
Biological Properties
General FunctionInvolved in FMN reductase activity
Specific FunctionHas several reductase activities that are NAD(P)H- dependent and involve FMN as a cofactor, ferricyanide being the best substrate for reduction. May be involved in ferric iron assimilation
Cellular LocationCytoplasm. Nucleus
SMPDB PathwaysNot Available
KEGG Pathways
Porphyrin and chlorophyll metabolismec00860 Map00860
SMPDB ReactionsNot Available
KEGG Reactions
NADH + Flavin Mononucleotide + hydron → NAD + FMNH2
Flavin Mononucleotide + NADPH + hydron → NADP + FMNH2
Metabolites
YMDB IDNameView
YMDB00085Flavin MononucleotideShow
YMDB00110NADShow
YMDB00143NADHShow
YMDB00412NAD(+)Show
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00686FMNH2Show
YMDB00862hydronShow
GO ClassificationNot Available
Gene Properties
Chromosome Locationchromosome 12
LocusYLR011W
Gene Sequence>576 bp ATGAAAGTGGGTATTATAATGGGTTCTGTGAGGGCAAAGAGGGTATGCCCAGAAATTGCA GCATACGTAAAACGTACAATTGAAAATAGCGAAGAATTAATAGACCAGAAGCTGAAAATA CAAGTAGTAGATTTACAACAGATTGCTCTTCCCTTATATGAAGATGATGACGAACTGATC CCTGCGCAAATAAAGAGCGTGGATGAGTATGCAGACAGCAAAACTCGATCGTGGAGTCGC ATCGTAAATGCATTAGATATTATTGTATTCGTTACACCTCAATATAATTGGGGGTATCCA GCAGCCTTAAAAAATGCAATTGATCGTCTTTACCATGAATGGCACGGAAAACCTGCCCTG GTGGTAAGCTACGGCGGTCATGGCGGTAGTAAGTGTAATGACCAACTTCAAGAGGTACTA CATGGTTTGAAGATGAATGTTATAGGTGGAGTGGCGGTGAAAATACCGGTAGGTACGATA CCGTTACCCGAGGACATTGTACCACAACTCAGCGTGCACAATGAAGAGATCCTGCAATTA CTCGCATCGTGCATCGAAACAACGAGGAATAAATAA
Protein Properties
Pfam Domain Function
Protein Residues191
Protein Molecular Weight21280.40039
Protein Theoretical pI6.01
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>NAD(P)H-dependent FMN reductase LOT6 MKVGIIMGSVRAKRVCPEIAAYVKRTIENSEELIDQKLKIQVVDLQQIALPLYEDDDELI PAQIKSVDEYADSKTRSWSRIVNALDIIVFVTPQYNWGYPAALKNAIDRLYHEWHGKPAL VVSYGGHGGSKCNDQLQEVLHGLKMNVIGGVAVKIPVGTIPLPEDIVPQLSVHNEEILQL LASCIETTRNK
References
External Links
ResourceLink
Saccharomyces Genome Database LOT6
Uniprot IDQ07923
Uniprot NameLOT6_YEAST
GenBank Gene IDAY558199
Genebank Protein ID45270288
PDB ID
1T0I
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
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Zhang, L., Ohta, A., Horiuchi, H., Takagi, M., Imai, R. (2001). "Multiple mechanisms regulate expression of low temperature responsive (LOT) genes in Saccharomyces cerevisiae." Biochem Biophys Res Commun 283:531-535.11327734
  • 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
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Liger, D., Graille, M., Zhou, C. Z., Leulliot, N., Quevillon-Cheruel, S., Blondeau, K., Janin, J., van Tilbeurgh, H. (2004). "Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities." J Biol Chem 279:34890-34897.15184374