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 03-AUG-2022, entry version 154.
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; 63.
DR DIP; DIP-4604N; -.
DR IntAct; Q07923; 1.
DR MINT; Q07923; -.
DR STRING; 4932.YLR011W; -.
DR MaxQB; Q07923; -.
DR PaxDb; Q07923; -.
DR PRIDE; Q07923; -.
DR EnsemblFungi; YLR011W_mRNA; YLR011W; YLR011W.
DR GeneID; 850698; -.
DR KEGG; sce:YLR011W; -.
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; PQYNWSV; -.
DR BioCyc; YEAST:G3O-32172-MON; -.
DR BRENDA; 1.6.5.2; 984.
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:0052874; F:FMN reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-EC.
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 GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IDA:SGD.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 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