2NDP_YEAST
ID 2NDP_YEAST Reviewed; 404 AA.
AC P47177; D6VWW7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative nitronate monooxygenase;
DE EC=1.13.12.16;
DE AltName: Full=Nitroalkane oxidase;
GN OrderedLocusNames=YJR149W; ORFNames=J2213;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 402.
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 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 [4]
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).
CC -!- FUNCTION: Catalyzes the oxidation of alkyl nitronates to produce the
CC corresponding carbonyl compounds and nitrites. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethylnitronate + O2 = acetaldehyde + chemical entity + H(+) +
CC nitrite; Xref=Rhea:RHEA:28767, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16301, ChEBI:CHEBI:24431,
CC ChEBI:CHEBI:77894; EC=1.13.12.16;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nitronate monooxygenase family. NMO class I
CC subfamily. {ECO:0000305}.
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DR EMBL; Z49649; CAA89682.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08933.2; -; Genomic_DNA.
DR PIR; S57178; S57178.
DR RefSeq; NP_012683.4; NM_001181807.4.
DR AlphaFoldDB; P47177; -.
DR SMR; P47177; -.
DR BioGRID; 33904; 71.
DR IntAct; P47177; 4.
DR MINT; P47177; -.
DR STRING; 4932.YJR149W; -.
DR PaxDb; P47177; -.
DR PRIDE; P47177; -.
DR EnsemblFungi; YJR149W_mRNA; YJR149W; YJR149W.
DR GeneID; 853614; -.
DR KEGG; sce:YJR149W; -.
DR SGD; S000003910; YJR149W.
DR VEuPathDB; FungiDB:YJR149W; -.
DR eggNOG; ENOG502S1Q4; Eukaryota.
DR HOGENOM; CLU_038732_5_0_1; -.
DR InParanoid; P47177; -.
DR OMA; FFCHEIE; -.
DR BioCyc; YEAST:G3O-31762-MON; -.
DR PRO; PR:P47177; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47177; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IBA:GO_Central.
DR CDD; cd04730; NPD_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR Pfam; PF03060; NMO; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flavoprotein; FMN; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..404
FT /note="Putative nitronate monooxygenase"
FT /id="PRO_0000203128"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 41..43
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270..272
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 293..294
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT CONFLICT 402
FT /note="D -> V (in Ref. 1; CAA89682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 45159 MW; E3FEE0E6C76ED7FA CRC64;
MYFLNQLIFQ DVSVMSVDKR EDMSRSFQKC LNLRYPIIQA PMAGVTTIEM AAKACIAGAI
ASLPLSHLDF RKVNDIEKLK LMVSQFRDQV ADESLEGNLN LNFFCHDIVD KPTDLQTANW
AKLYRKSMNV PIDMNEIKFD NGNVSFKAFE KENALQDFFQ YLSDGFRPKI ISFHFGHPSK
STIEYLQKIG ILIFVTATSV REVRLLARLG INGIVCQGYE AGGHRGNFLV NDPKDDENLS
TVQLVKRTVD ELAEMKNKGL IHATPFVIAA GGIMDSKDIS YMLSQQADAV QVGTAFLGCS
ESNASKNFSS PFTRETTTKM VNIISGKPAR TISTPFIEKV IANFQGEELP PYGYMYSAFK
QVRKKYPELA NFILAGQGFQ NVQSGITTDK KIETMGARLK IDGK
