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Database: UniProt
Entry: LOT6_YEAST
LinkDB: LOT6_YEAST
Original site: LOT6_YEAST 
ID   LOT6_YEAST              Reviewed;         191 AA.
AC   Q07923; D6VY13;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=NAD(P)H-dependent FMN reductase LOT6;
DE            Short=FMN reductase LOT6;
DE            EC=1.5.1.39;
DE   AltName: Full=Azoreductase LOT6;
DE   AltName: Full=FMN reductase [NAD(P)H];
DE   AltName: Full=Low temperature response protein 6;
GN   Name=LOT6; OrderedLocusNames=YLR011W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   INDUCTION.
RX   PubMed=11327734; DOI=10.1006/bbrc.2001.4776;
RA   Zhang L., Ohta A., Horiuchi H., Takagi M., Imai R.;
RT   "Multiple mechanisms regulate expression of low temperature responsive
RT   (LOT) genes in Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 283:531-535(2001).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX   PubMed=15184374; DOI=10.1074/jbc.m405404200;
RA   Liger D., Graille M., Zhou C.-Z., Leulliot N., Quevillon-Cheruel S.,
RA   Blondeau K., Janin J., van Tilbeurgh H.;
RT   "Crystal structure and functional characterization of yeast YLR011wp, an
RT   enzyme with NAD(P)H-FMN and ferric iron reductase activities.";
RL   J. Biol. Chem. 279:34890-34897(2004).
CC   -!- FUNCTION: Has several reductase activities that are NAD(P)H-dependent
CC       and involve FMN as a cofactor, ferricyanide being the best substrate
CC       for reduction. May be involved in ferric iron assimilation.
CC       {ECO:0000269|PubMed:15184374}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.39;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.39;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15184374}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Induced by low temperature and by cycloheximide.
CC       {ECO:0000269|PubMed:11327734}.
CC   -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z73183; CAA97533.1; -; Genomic_DNA.
DR   EMBL; AY558199; AAS56525.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09329.1; -; Genomic_DNA.
DR   PIR; S64833; S64833.
DR   RefSeq; NP_013111.1; NM_001181898.1.
DR   PDB; 1T0I; X-ray; 2.00 A; A/B=1-191.
DR   PDBsum; 1T0I; -.
DR   AlphaFoldDB; Q07923; -.
DR   SMR; Q07923; -.
DR   BioGRID; 31285; 66.
DR   DIP; DIP-4604N; -.
DR   IntAct; Q07923; 1.
DR   MINT; Q07923; -.
DR   STRING; 4932.YLR011W; -.
DR   MaxQB; Q07923; -.
DR   PaxDb; 4932-YLR011W; -.
DR   PeptideAtlas; Q07923; -.
DR   EnsemblFungi; YLR011W_mRNA; YLR011W; YLR011W.
DR   GeneID; 850698; -.
DR   KEGG; sce:YLR011W; -.
DR   AGR; SGD:S000004001; -.
DR   SGD; S000004001; LOT6.
DR   VEuPathDB; FungiDB:YLR011W; -.
DR   eggNOG; KOG4530; Eukaryota.
DR   GeneTree; ENSGT00390000005275; -.
DR   HOGENOM; CLU_055322_2_1_1; -.
DR   InParanoid; Q07923; -.
DR   OMA; LFHEWAG; -.
DR   OrthoDB; 73508at2759; -.
DR   BioCyc; YEAST:G3O-32172-MONOMER; -.
DR   BRENDA; 1.6.5.2; 984.
DR   BioGRID-ORCS; 850698; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q07923; -.
DR   PRO; PR:Q07923; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q07923; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0008752; F:FMN reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR   GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:RHEA.
DR   GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:SGD.
DR   GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   PANTHER; PTHR30543; CHROMATE REDUCTASE; 1.
DR   PANTHER; PTHR30543:SF21; NAD(P)H-DEPENDENT FMN REDUCTASE LOT6; 1.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Flavoprotein; FMN; NAD; NADP; Nucleus;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..191
FT                   /note="NAD(P)H-dependent FMN reductase LOT6"
FT                   /id="PRO_0000234661"
FT   BINDING         11
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   BINDING         94..97
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   BINDING         124
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           16..28
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   TURN            31..37
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           45..48
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           73..83
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           101..108
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   TURN            112..116
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   STRAND          118..125
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   TURN            126..129
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           130..142
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   STRAND          146..154
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   TURN            164..166
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           168..173
FT                   /evidence="ECO:0007829|PDB:1T0I"
FT   HELIX           174..184
FT                   /evidence="ECO:0007829|PDB:1T0I"
SQ   SEQUENCE   191 AA;  21281 MW;  90C8FD4A39BA2FB7 CRC64;
     MKVGIIMGSV RAKRVCPEIA AYVKRTIENS EELIDQKLKI QVVDLQQIAL PLYEDDDELI
     PAQIKSVDEY ADSKTRSWSR IVNALDIIVF VTPQYNWGYP AALKNAIDRL YHEWHGKPAL
     VVSYGGHGGS KCNDQLQEVL HGLKMNVIGG VAVKIPVGTI PLPEDIVPQL SVHNEEILQL
     LASCIETTRN K
//
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