FMO1_YEAST
ID FMO1_YEAST Reviewed; 432 AA.
AC P38866; D3DLC5; Q6UZ93;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Thiol-specific monooxygenase;
DE EC=1.14.13.-;
DE AltName: Full=Flavin-dependent monooxygenase;
GN Name=FMO1; OrderedLocusNames=YHR176W;
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 [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=12139977; DOI=10.1016/s0003-9861(02)00237-0;
RA Zhang M., Robertus J.D.;
RT "Molecular cloning and characterization of a full-length flavin-dependent
RT monooxygenase from yeast.";
RL Arch. Biochem. Biophys. 403:277-283(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Fisk D., Cherry J.M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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).
CC -!- FUNCTION: Flavin-dependent oxidation of thiol-containing compounds.
CC Probably required for the correct folding of disulfide-bonded proteins.
CC {ECO:0000269|PubMed:12139977}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12139977}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AY357258; AAQ62539.1; -; Genomic_DNA.
DR EMBL; U00027; AAB68021.2; -; Genomic_DNA.
DR EMBL; BK006934; DAA06869.1; -; Genomic_DNA.
DR PIR; S48915; S48915.
DR RefSeq; NP_012046.4; NM_001179307.3.
DR AlphaFoldDB; P38866; -.
DR SMR; P38866; -.
DR BioGRID; 36609; 49.
DR IntAct; P38866; 1.
DR STRING; 4932.YHR176W; -.
DR MaxQB; P38866; -.
DR PaxDb; P38866; -.
DR PRIDE; P38866; -.
DR EnsemblFungi; YHR176W_mRNA; YHR176W; YHR176W.
DR GeneID; 856581; -.
DR KEGG; sce:YHR176W; -.
DR SGD; S000001219; FMO1.
DR VEuPathDB; FungiDB:YHR176W; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_0_1; -.
DR InParanoid; P38866; -.
DR OMA; FMEWEHH; -.
DR BioCyc; YEAST:G3O-31209-MON; -.
DR PRO; PR:P38866; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38866; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IDA:SGD.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 2.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..432
FT /note="Thiol-specific monooxygenase"
FT /id="PRO_0000147670"
FT BINDING 13..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 46..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 65..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 117..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 199..202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
SQ SEQUENCE 432 AA; 49099 MW; 813C1B2BC196FA60 CRC64;
MTVNDKKRLA IIGGGPGGLA AARVFSQSLP NFEIEIFVKD YDIGGVWHYP EQKSDGRVMY
DHLETNISKK LMQFSGFPFE ENVPLYPSRR NIWEYLKAYY KTFIANKDAI SIHFSTEVTY
LKKKNSQWEI TSKDELRTTK SDFDFVIVAS GHYSVPKLPT NIAGLDLWFD NKGAFHSKDF
KNCEFAREKV VIVVGNGSSG QDIANQLTTV AKKVYNSIKE PASNQLKAKL IETVQTIDSA
DWKNRSVTLS DGRVLQNIDY IIFATGYYYS FPFIEPSVRL EVLGEGVTGD KHSSVNLHNL
WEHMIYVKDP TLSFILTPQL VIPFPLSELQ AAIMVEVFCK SLPITTTFDS NACGTHNFPK
GKDLEYYAEL QELLNSIPRR VGHFEPVVWD DRLIDLRNSS YTDKEERNVL LAEHAQALKK
KKAPYFLPAP HT
