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Protein

Polyamine oxidase FMS1

Gene

FMS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.2 Publications

Catalytic activityi

Spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2.1 Publication
Spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2.1 Publication
N(1)-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2.1 Publication
N(1)-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2.1 Publication
N(8)-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2.1 Publication

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

GO - Molecular functioni

GO - Biological processi

  • pantothenate biosynthetic process Source: SGD
  • spermine catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13663.
YEAST:YMR020W-MONOMER.
BRENDAi1.5.3.17. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyamine oxidase FMS1 (EC:1.5.3.171 Publication)
Alternative name(s):
Fenpropimorph resistance multicopy suppressor 1
Gene namesi
Name:FMS1
Ordered Locus Names:YMR020W
ORF Names:YM9711.09
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR020W.
SGDiS000004622. FMS1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Polyamine oxidase FMS1PRO_0000087317Add
BLAST

Proteomic databases

MaxQBiP50264.

Interactioni

Protein-protein interaction databases

BioGridi35191. 36 interactions.
DIPiDIP-3959N.
MINTiMINT-492079.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Helixi18 – 2912Combined sources
Beta strandi34 – 385Combined sources
Beta strandi40 – 456Combined sources
Beta strandi50 – 523Combined sources
Helixi54 – 563Combined sources
Beta strandi58 – 625Combined sources
Turni69 – 713Combined sources
Helixi73 – 8513Combined sources
Beta strandi90 – 923Combined sources
Beta strandi98 – 1014Combined sources
Turni102 – 1043Combined sources
Turni111 – 1133Combined sources
Helixi115 – 12915Combined sources
Turni131 – 1344Combined sources
Helixi141 – 15212Combined sources
Helixi153 – 1553Combined sources
Helixi158 – 16811Combined sources
Helixi169 – 1713Combined sources
Helixi172 – 1754Combined sources
Turni179 – 1813Combined sources
Helixi184 – 1874Combined sources
Beta strandi196 – 1994Combined sources
Helixi201 – 2099Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi223 – 2286Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi243 – 2519Combined sources
Helixi255 – 2595Combined sources
Helixi260 – 2623Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi273 – 2764Combined sources
Helixi280 – 2856Combined sources
Helixi286 – 2883Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi295 – 3039Combined sources
Beta strandi311 – 3155Combined sources
Helixi321 – 3299Combined sources
Helixi333 – 3397Combined sources
Helixi353 – 3553Combined sources
Beta strandi358 – 3625Combined sources
Helixi363 – 3664Combined sources
Beta strandi370 – 3767Combined sources
Helixi380 – 3867Combined sources
Turni387 – 3893Combined sources
Helixi391 – 40818Combined sources
Helixi420 – 4223Combined sources
Helixi424 – 4263Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi431 – 4377Combined sources
Turni440 – 4423Combined sources
Turni444 – 4485Combined sources
Helixi461 – 4688Combined sources
Beta strandi470 – 4767Combined sources
Helixi479 – 4813Combined sources
Turni484 – 4874Combined sources
Helixi489 – 50820Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RSGX-ray1.90A/B1-508[»]
1XPQX-ray2.60A/B/C/D1-508[»]
1YY5X-ray2.30A/B1-508[»]
1Z6LX-ray2.50A/B1-508[»]
3BI2X-ray2.30A/B1-508[»]
3BI4X-ray2.20A/B1-508[»]
3BI5X-ray2.50A/B1-508[»]
3BNMX-ray2.20A/B1-508[»]
3BNUX-ray2.20A/B1-508[»]
3CN8X-ray2.40A/B1-508[»]
3CNDX-ray2.50A/B1-508[»]
3CNPX-ray2.50A/B1-508[»]
3CNSX-ray2.40A/B1-508[»]
3CNTX-ray2.70A/B1-508[»]
4ECHX-ray2.40A/B1-508[»]
4GDPX-ray2.00A/B/C/D1-508[»]
ProteinModelPortaliP50264.
SMRiP50264. Positions 7-508.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50264.

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Phylogenomic databases

HOGENOMiHOG000246632.
InParanoidiP50264.
KOiK13367.
OrthoDBiEOG78D7V2.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P50264-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTVSPAKKK VIIIGAGIAG LKAASTLHQN GIQDCLVLEA RDRVGGRLQT
60 70 80 90 100
VTGYQGRKYD IGASWHHDTL TNPLFLEEAQ LSLNDGRTRF VFDDDNFIYI
110 120 130 140 150
DEERGRVDHD KELLLEIVDN EMSKFAELEF HQHLGVSDCS FFQLVMKYLL
160 170 180 190 200
QRRQFLTNDQ IRYLPQLCRY LELWHGLDWK LLSAKDTYFG HQGRNAFALN
210 220 230 240 250
YDSVVQRIAQ SFPQNWLKLS CEVKSITREP SKNVTVNCED GTVYNADYVI
260 270 280 290 300
ITVPQSVLNL SVQPEKNLRG RIEFQPPLKP VIQDAFDKIH FGALGKVIFE
310 320 330 340 350
FEECCWSNES SKIVTLANST NEFVEIVRNA ENLDELDSML EREDSQKHTS
360 370 380 390 400
VTCWSQPLFF VNLSKSTGVA SFMMLMQAPL TNHIESIRED KERLFSFFQP
410 420 430 440 450
VLNKIMKCLD SEDVIDGMRP IENIANANKP VLRNIIVSNW TRDPYSRGAY
460 470 480 490 500
SACFPGDDPV DMVVAMSNGQ DSRIRFAGEH TIMDGAGCAY GAWESGRREA

TRISDLLK
Length:508
Mass (Da):57,806
Last modified:October 1, 1996 - v1
Checksum:i8E135295301EB3CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81848 Genomic DNA. Translation: CAA57442.1.
Z49211 Genomic DNA. Translation: CAA89122.1.
BK006946 Genomic DNA. Translation: DAA09918.1.
PIRiS54021.
RefSeqiNP_013733.1. NM_001182516.1.

Genome annotation databases

EnsemblFungiiYMR020W; YMR020W; YMR020W.
GeneIDi855034.
KEGGisce:YMR020W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81848 Genomic DNA. Translation: CAA57442.1.
Z49211 Genomic DNA. Translation: CAA89122.1.
BK006946 Genomic DNA. Translation: DAA09918.1.
PIRiS54021.
RefSeqiNP_013733.1. NM_001182516.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RSGX-ray1.90A/B1-508[»]
1XPQX-ray2.60A/B/C/D1-508[»]
1YY5X-ray2.30A/B1-508[»]
1Z6LX-ray2.50A/B1-508[»]
3BI2X-ray2.30A/B1-508[»]
3BI4X-ray2.20A/B1-508[»]
3BI5X-ray2.50A/B1-508[»]
3BNMX-ray2.20A/B1-508[»]
3BNUX-ray2.20A/B1-508[»]
3CN8X-ray2.40A/B1-508[»]
3CNDX-ray2.50A/B1-508[»]
3CNPX-ray2.50A/B1-508[»]
3CNSX-ray2.40A/B1-508[»]
3CNTX-ray2.70A/B1-508[»]
4ECHX-ray2.40A/B1-508[»]
4GDPX-ray2.00A/B/C/D1-508[»]
ProteinModelPortaliP50264.
SMRiP50264. Positions 7-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35191. 36 interactions.
DIPiDIP-3959N.
MINTiMINT-492079.

Proteomic databases

MaxQBiP50264.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR020W; YMR020W; YMR020W.
GeneIDi855034.
KEGGisce:YMR020W.

Organism-specific databases

EuPathDBiFungiDB:YMR020W.
SGDiS000004622. FMS1.

Phylogenomic databases

HOGENOMiHOG000246632.
InParanoidiP50264.
KOiK13367.
OrthoDBiEOG78D7V2.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13663.
YEAST:YMR020W-MONOMER.
BRENDAi1.5.3.17. 984.

Miscellaneous databases

EvolutionaryTraceiP50264.
PROiP50264.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the Saccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1."
    Joets J., Pousset D., Marcireau C., Karst F.
    Curr. Genet. 30:115-120(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase."
    Chattopadhyay M.K., Tabor C.W., Tabor H.
    Proc. Natl. Acad. Sci. U.S.A. 100:13869-13874(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiFMS1_YEAST
AccessioniPrimary (citable) accession number: P50264
Secondary accession number(s): D6VZJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6960 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.