ID   LOT6_YEAST              Reviewed;         191 AA.
AC   Q07923;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=NAD(P)H-dependent FMN reductase LOT6;
DE            Short=FMN reductase LOT6;
DE            EC=1.5.1.29;
DE   AltName: Full=Azoreductase LOT6;
DE   AltName: Full=Low temperature response protein 6;
GN   Name=LOT6; OrderedLocusNames=YLR011W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
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   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
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,
RT   an 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-
CC       dependent and involve FMN as a cofactor, ferricyanide being the
CC       best substrate for reduction. May be involved in ferric iron
CC       assimilation.
CC   -!- CATALYTIC ACTIVITY: FMNH(2) + NAD(P)(+) = FMN + NAD(P)H.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P38800:-; NbExp=1; IntAct=EBI-31608, EBI-24597;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- INDUCTION: Induced by low temperature and by cycloheximide.
CC   -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD
CC       medium.
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DR   EMBL; Z73183; CAA97533.1; -; Genomic_DNA.
DR   EMBL; AY558199; AAS56525.1; -; Genomic_DNA.
DR   PIR; S64833; S64833.
DR   RefSeq; NP_013111.1; -.
DR   PDB; 1T0I; X-ray; 2.00 A; A/B=1-191.
DR   PDBsum; 1T0I; -.
DR   DIP; DIP:4604N; -.
DR   IntAct; Q07923; 3.
DR   PRIDE; Q07923; -.
DR   Ensembl; YLR011W; Saccharomyces cerevisiae.
DR   GeneID; 850698; -.
DR   GenomeReviews; Y13138_GR; YLR011W.
DR   KEGG; sce:YLR011W; -.
DR   NMPDR; fig|4932.3.peg.4102; -.
DR   CYGD; YLR011w; -.
DR   SGD; S000004001; LOT6.
DR   HOGENOM; Q07923; -.
DR   OMA; Q07923; AVELQMA.
DR   BRENDA; 1.5.1.29; 250.
DR   NextBio; 966730; -.
DR   ArrayExpress; Q07923; -.
DR   GermOnline; YLR011W; Saccharomyces cerevisiae.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:EC.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:SGD.
DR   GO; GO:0008134; F:transcription factor binding; IDA:SGD.
DR   GO; GO:0042994; P:cytoplasmic sequestering of transcription f...; IDA:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR   InterPro; IPR005025; FMN_red.
DR   Pfam; PF03358; FMN_red; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Flavoprotein; FMN; NAD;
KW   NADP; Nucleus; Oxidoreductase.
FT   CHAIN         1    191       NAD(P)H-dependent FMN reductase LOT6.
FT                                /FTId=PRO_0000234661.
FT   REGION       94     97       FMN binding.
FT   BINDING      11     11       FMN.
FT   BINDING     124    124       FMN.
FT   STRAND        2      7
FT   HELIX        16     28
FT   TURN         31     37
FT   STRAND       39     43
FT   HELIX        45     48
FT   HELIX        61     63
FT   HELIX        67     69
FT   HELIX        73     83
FT   STRAND       86     93
FT   HELIX       101    108
FT   TURN        112    116
FT   STRAND      118    125
FT   TURN        126    129
FT   HELIX       130    142
FT   STRAND      146    154
FT   TURN        164    166
FT   HELIX       168    173
FT   HELIX       174    184
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
//