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UniProtKB/Swiss-Prot entry Q07923


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LOT6_YEAST
Primary accession number Q07923
Secondary accession numbers None
Integrated into Swiss-Prot on May 16, 2006
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 48)
Name and origin of the protein
Protein name NAD(P)H-dependent FMN reductase LOT6
Synonyms FMN reductase LOT6
EC 1.5.1.29
Azoreductase LOT6
Low temperature response protein 6
Gene name
Name: LOT6
OrderedLocusNames: YLR011W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., 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.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[3]
INDUCTION.
DOI=10.1006/bbrc.2001.4776; PubMed=11327734 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang L., Ohta A., Horiuchi H., Takagi M., Imai R.;
"Multiple mechanisms regulate expression of low temperature responsive (LOT) genes in Saccharomyces cerevisiae.";
Biochem. Biophys. Res. Commun. 283:531-535(2001).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, AND SUBUNIT.
DOI=10.1074/jbc.M405404200; PubMed=15184374 [NCBI, ExPASy, EBI, Israel, Japan]
Liger D., Graille M., Zhou C.-Z., Leulliot N., Quevillon-Cheruel S., Blondeau K., Janin J., van Tilbeurgh H.;
"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(2004).
Comments
  • FUNCTION: Has 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.
  • CATALYTIC ACTIVITY: FMNH2 + NAD(P)+ = FMN + NAD(P)H.
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • INDUCTION: Induced by low temperature and by cycloheximide.
  • MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z73183; CAA97533.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558199; AAS56525.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64833; S64833.
RefSeq NP_013111.1; -.
3D structure databases
PDB
1T0I; X-ray; 2.00 A; A/B=1-191.[ExPASy / RCSB / EBI]
PDBsum 1T0I; -.
ModBase Q07923.
Protein-protein interaction databases
DIP DIP:4604N; -.
IntAct Q07923; 2.
Organism-specific databases
CYGD YLR011w; -.
SGD S000004001; LOT6.
Yeast-GFP YLR011W.
Gene expression databases
ArrayExpress Q07923; -.
GermOnline YLR011W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0008752; Molecular function: FMN reductase activity (inferred from electronic annotation from EC).
GO:0003955; Molecular function: NAD(P)H dehydrogenase (quinone) activity (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979; Biological process: response to oxidative stress (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR005025; FMN_red.
Graphical view of domain structure.
Pfam PF03358; FMN_red; 1.
Pfam graphical view of domain structure.
Genome annotation databases
Ensembl YLR011W; Saccharomyces cerevisiae. [Contig view]
GeneID 850698; -.
GenomeReviews Y13138_GR; YLR011W.
KEGG sce:YLR011W; -.
NMPDR fig|4932.3.peg.4102; -.
Phylogenomic databases
HOGENOM Q07923; -.
Other
LinkHub Q07923; -.
NextBio 966730; -.
ProtoNet Q07923.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Flavoprotein; FMN; NAD; NADP; Nucleus; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   191  191     NAD(P)H-dependent FMN reductase LOT6. PRO_0000234661
REGION   94    97  4     FMN binding. 
BINDING   11    11        FMN. 
BINDING   124   124        FMN. 
STRAND   2     7  6      
HELIX   16    28  13      
TURN   31    37  7      
STRAND   39    43  5      
HELIX   45    48  4      
HELIX   61    63  3      
HELIX   67    69  3      
HELIX   73    83  11      
STRAND   86    93  8      
HELIX   101   108  8      
TURN   112   116  5      
STRAND   118   125  8      
TURN   126   129  4      
HELIX   130   142  13      
STRAND   146   154  9      
TURN   164   166  3      
HELIX   168   173  6      
HELIX   174   184  11      
Sequence information
Length: 191 AA [This is the length of the unprocessed precursor] Molecular weight: 21281 Da [This is the MW of the unprocessed precursor] CRC64: 90C8FD4A39BA2FB7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKVGIIMGSV RAKRVCPEIA AYVKRTIENS EELIDQKLKI QVVDLQQIAL PLYEDDDELI 

        70         80         90        100        110        120 
PAQIKSVDEY ADSKTRSWSR IVNALDIIVF VTPQYNWGYP AALKNAIDRL YHEWHGKPAL 

       130        140        150        160        170        180 
VVSYGGHGGS KCNDQLQEVL HGLKMNVIGG VAVKIPVGTI PLPEDIVPQL SVHNEEILQL 

       190 
LASCIETTRN K 

Q07923 in FASTA format

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