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Protein

NAD(P)H-dependent FMN reductase LOT6

Gene

LOT6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

FMNH2 + NAD(P)+ = FMN + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111FMN
Binding sitei124 – 1241FMN

GO - Molecular functioni

  • FMN reductase (NADH) activity Source: UniProtKB-EC
  • FMN reductase (NADPH) activity Source: UniProtKB-EC
  • NAD(P)H dehydrogenase (quinone) activity Source: SGD
  • transcription factor binding Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • cellular response to oxidative stress Source: SGD
  • cytoplasmic sequestering of transcription factor Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NAD, NADP

Enzyme and pathway databases

BioCyciYEAST:G3O-32172-MONOMER.
BRENDAi1.6.5.2. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)H-dependent FMN reductase LOT6 (EC:1.5.1.39)
Short name:
FMN reductase LOT6
Alternative name(s):
Azoreductase LOT6
FMN reductase [NAD(P)H]
Low temperature response protein 6
Gene namesi
Name:LOT6
Ordered Locus Names:YLR011W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR011W.
SGDiS000004001. LOT6.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191NAD(P)H-dependent FMN reductase LOT6PRO_0000234661Add
BLAST

Proteomic databases

MaxQBiQ07923.

Expressioni

Inductioni

Induced by low temperature and by cycloheximide.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi31285. 17 interactions.
DIPiDIP-4604N.
IntActiQ07923. 1 interaction.
MINTiMINT-568995.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi16 – 2813Combined sources
Turni31 – 377Combined sources
Beta strandi39 – 435Combined sources
Helixi45 – 484Combined sources
Helixi61 – 633Combined sources
Helixi67 – 693Combined sources
Helixi73 – 8311Combined sources
Beta strandi86 – 938Combined sources
Helixi101 – 1088Combined sources
Turni112 – 1165Combined sources
Beta strandi118 – 1258Combined sources
Turni126 – 1294Combined sources
Helixi130 – 14213Combined sources
Beta strandi146 – 1549Combined sources
Turni164 – 1663Combined sources
Helixi168 – 1736Combined sources
Helixi174 – 18411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T0IX-ray2.00A/B1-191[»]
ProteinModelPortaliQ07923.
SMRiQ07923. Positions 1-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07923.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 974FMN binding

Phylogenomic databases

HOGENOMiHOG000263121.
InParanoidiQ07923.
OMAiSAVHIAW.
OrthoDBiEOG7D5B08.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR029039. Flavoprotein-like_dom.
IPR005025. FMN_Rdtase-like.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.

Sequencei

Sequence statusi: Complete.

Q07923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVGIIMGSV RAKRVCPEIA AYVKRTIENS EELIDQKLKI QVVDLQQIAL
60 70 80 90 100
PLYEDDDELI PAQIKSVDEY ADSKTRSWSR IVNALDIIVF VTPQYNWGYP
110 120 130 140 150
AALKNAIDRL YHEWHGKPAL VVSYGGHGGS KCNDQLQEVL HGLKMNVIGG
160 170 180 190
VAVKIPVGTI PLPEDIVPQL SVHNEEILQL LASCIETTRN K
Length:191
Mass (Da):21,281
Last modified:November 1, 1996 - v1
Checksum:i90C8FD4A39BA2FB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73183 Genomic DNA. Translation: CAA97533.1.
AY558199 Genomic DNA. Translation: AAS56525.1.
BK006945 Genomic DNA. Translation: DAA09329.1.
PIRiS64833.
RefSeqiNP_013111.1. NM_001181898.1.

Genome annotation databases

EnsemblFungiiYLR011W; YLR011W; YLR011W.
GeneIDi850698.
KEGGisce:YLR011W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73183 Genomic DNA. Translation: CAA97533.1.
AY558199 Genomic DNA. Translation: AAS56525.1.
BK006945 Genomic DNA. Translation: DAA09329.1.
PIRiS64833.
RefSeqiNP_013111.1. NM_001181898.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T0IX-ray2.00A/B1-191[»]
ProteinModelPortaliQ07923.
SMRiQ07923. Positions 1-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31285. 17 interactions.
DIPiDIP-4604N.
IntActiQ07923. 1 interaction.
MINTiMINT-568995.

Proteomic databases

MaxQBiQ07923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR011W; YLR011W; YLR011W.
GeneIDi850698.
KEGGisce:YLR011W.

Organism-specific databases

EuPathDBiFungiDB:YLR011W.
SGDiS000004001. LOT6.

Phylogenomic databases

HOGENOMiHOG000263121.
InParanoidiQ07923.
OMAiSAVHIAW.
OrthoDBiEOG7D5B08.

Enzyme and pathway databases

BioCyciYEAST:G3O-32172-MONOMER.
BRENDAi1.6.5.2. 984.

Miscellaneous databases

EvolutionaryTraceiQ07923.
NextBioi966730.
PROiQ07923.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR029039. Flavoprotein-like_dom.
IPR005025. FMN_Rdtase-like.
[Graphical view]
PfamiPF03358. FMN_red. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    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.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Multiple mechanisms regulate expression of low temperature responsive (LOT) genes in Saccharomyces cerevisiae."
    Zhang L., Ohta A., Horiuchi H., Takagi M., Imai R.
    Biochem. Biophys. Res. Commun. 283:531-535(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities."
    Liger D., Graille M., Zhou C.-Z., Leulliot N., Quevillon-Cheruel S., Blondeau K., Janin J., van Tilbeurgh H.
    J. Biol. Chem. 279:34890-34897(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, SUBUNIT.

Entry informationi

Entry nameiLOT6_YEAST
AccessioniPrimary (citable) accession number: Q07923
Secondary accession number(s): D6VY13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1270 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.