FMS1_YEAST
ID FMS1_YEAST Reviewed; 508 AA.
AC P50264; D6VZJ4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Polyamine oxidase FMS1;
DE EC=1.5.3.17 {ECO:0000269|PubMed:12670477};
DE AltName: Full=Fenpropimorph resistance multicopy suppressor 1;
GN Name=FMS1; OrderedLocusNames=YMR020W; ORFNames=YM9711.09;
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].
RX PubMed=8660467; DOI=10.1007/s002940050109;
RA Joets J., Pousset D., Marcireau C., Karst F.;
RT "Characterization of the Saccharomyces cerevisiae FMS1 gene related to
RT Candida albicans corticosteroid-binding protein 1.";
RL Curr. Genet. 30:115-120(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=12670477; DOI=10.1016/s0006-291x(03)00416-9;
RA Landry J., Sternglanz R.;
RT "Yeast Fms1 is a FAD-utilizing polyamine oxidase.";
RL Biochem. Biophys. Res. Commun. 303:771-776(2003).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=14617780; DOI=10.1073/pnas.1835918100;
RA Chattopadhyay M.K., Tabor C.W., Tabor H.;
RT "Spermidine but not spermine is essential for hypusine biosynthesis and
RT growth in Saccharomyces cerevisiae: spermine is converted to spermidine in
RT vivo by the FMS1-amine oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13869-13874(2003).
CC -!- FUNCTION: Involved in the production of beta-alanine, a precursor of
CC pantothenic acid. Multicopy suppressor of fenpropimorph resistance.
CC {ECO:0000269|PubMed:12670477, ECO:0000269|PubMed:14617780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine;
CC Xref=Rhea:RHEA:25804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:45725, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:58374; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:12670477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + spermidine = 3-aminopropanal + H2O2 + putrescine;
CC Xref=Rhea:RHEA:25808, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57834, ChEBI:CHEBI:58374,
CC ChEBI:CHEBI:326268; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:12670477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 +
CC spermidine; Xref=Rhea:RHEA:25800, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58101; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:12670477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2
CC + putrescine; Xref=Rhea:RHEA:25812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:58324, ChEBI:CHEBI:326268; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:12670477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 +
CC propane-1,3-diamine; Xref=Rhea:RHEA:25972, ChEBI:CHEBI:7386,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57484, ChEBI:CHEBI:58535; EC=1.5.3.17;
CC Evidence={ECO:0000269|PubMed:12670477};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12670477};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:12670477};
CC -!- MISCELLANEOUS: Present with 6960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; X81848; CAA57442.1; -; Genomic_DNA.
DR EMBL; Z49211; CAA89122.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09918.1; -; Genomic_DNA.
DR PIR; S54021; S54021.
DR RefSeq; NP_013733.1; NM_001182516.1.
DR PDB; 1RSG; X-ray; 1.90 A; A/B=1-508.
DR PDB; 1XPQ; X-ray; 2.60 A; A/B/C/D=1-508.
DR PDB; 1YY5; X-ray; 2.30 A; A/B=1-508.
DR PDB; 1Z6L; X-ray; 2.50 A; A/B=1-508.
DR PDB; 3BI2; X-ray; 2.30 A; A/B=1-508.
DR PDB; 3BI4; X-ray; 2.20 A; A/B=1-508.
DR PDB; 3BI5; X-ray; 2.50 A; A/B=1-508.
DR PDB; 3BNM; X-ray; 2.20 A; A/B=1-508.
DR PDB; 3BNU; X-ray; 2.20 A; A/B=1-508.
DR PDB; 3CN8; X-ray; 2.40 A; A/B=1-508.
DR PDB; 3CND; X-ray; 2.50 A; A/B=1-508.
DR PDB; 3CNP; X-ray; 2.50 A; A/B=1-508.
DR PDB; 3CNS; X-ray; 2.40 A; A/B=1-508.
DR PDB; 3CNT; X-ray; 2.70 A; A/B=1-508.
DR PDB; 4ECH; X-ray; 2.40 A; A/B=1-508.
DR PDB; 4GDP; X-ray; 2.00 A; A/B/C/D=1-508.
DR PDBsum; 1RSG; -.
DR PDBsum; 1XPQ; -.
DR PDBsum; 1YY5; -.
DR PDBsum; 1Z6L; -.
DR PDBsum; 3BI2; -.
DR PDBsum; 3BI4; -.
DR PDBsum; 3BI5; -.
DR PDBsum; 3BNM; -.
DR PDBsum; 3BNU; -.
DR PDBsum; 3CN8; -.
DR PDBsum; 3CND; -.
DR PDBsum; 3CNP; -.
DR PDBsum; 3CNS; -.
DR PDBsum; 3CNT; -.
DR PDBsum; 4ECH; -.
DR PDBsum; 4GDP; -.
DR AlphaFoldDB; P50264; -.
DR SMR; P50264; -.
DR BioGRID; 35191; 74.
DR DIP; DIP-3959N; -.
DR MINT; P50264; -.
DR STRING; 4932.YMR020W; -.
DR MaxQB; P50264; -.
DR PaxDb; P50264; -.
DR PRIDE; P50264; -.
DR EnsemblFungi; YMR020W_mRNA; YMR020W; YMR020W.
DR GeneID; 855034; -.
DR KEGG; sce:YMR020W; -.
DR SGD; S000004622; FMS1.
DR VEuPathDB; FungiDB:YMR020W; -.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000174336; -.
DR HOGENOM; CLU_004498_10_1_1; -.
DR InParanoid; P50264; -.
DR OMA; EFFDNYQ; -.
DR BioCyc; MetaCyc:YMR020W-MON; -.
DR BioCyc; YEAST:YMR020W-MON; -.
DR BRENDA; 1.5.3.17; 984.
DR Reactome; R-SCE-3214842; HDMs demethylate histones.
DR EvolutionaryTrace; P50264; -.
DR PRO; PR:P50264; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50264; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052897; F:N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity; IEA:RHEA.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IDA:SGD.
DR GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:SGD.
DR GO; GO:0046208; P:spermine catabolic process; IMP:SGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..508
FT /note="Polyamine oxidase FMS1"
FT /id="PRO_0000087317"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4ECH"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:3BNM"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3BNU"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4GDP"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3CNT"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:3CND"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4GDP"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3BI4"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4ECH"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 391..408
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:4GDP"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3CN8"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:1RSG"
FT TURN 444..448
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:1RSG"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:1RSG"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:3BI4"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:4GDP"
FT HELIX 489..508
FT /evidence="ECO:0007829|PDB:1RSG"
SQ SEQUENCE 508 AA; 57806 MW; 8E135295301EB3CF CRC64;
MNTVSPAKKK VIIIGAGIAG LKAASTLHQN GIQDCLVLEA RDRVGGRLQT VTGYQGRKYD
IGASWHHDTL TNPLFLEEAQ LSLNDGRTRF VFDDDNFIYI DEERGRVDHD KELLLEIVDN
EMSKFAELEF HQHLGVSDCS FFQLVMKYLL QRRQFLTNDQ IRYLPQLCRY LELWHGLDWK
LLSAKDTYFG HQGRNAFALN YDSVVQRIAQ SFPQNWLKLS CEVKSITREP SKNVTVNCED
GTVYNADYVI ITVPQSVLNL SVQPEKNLRG RIEFQPPLKP VIQDAFDKIH FGALGKVIFE
FEECCWSNES SKIVTLANST NEFVEIVRNA ENLDELDSML EREDSQKHTS VTCWSQPLFF
VNLSKSTGVA SFMMLMQAPL TNHIESIRED KERLFSFFQP VLNKIMKCLD SEDVIDGMRP
IENIANANKP VLRNIIVSNW TRDPYSRGAY SACFPGDDPV DMVVAMSNGQ DSRIRFAGEH
TIMDGAGCAY GAWESGRREA TRISDLLK
