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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:YMR020W-MONOMER.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00000873171 – 508Polyamine oxidase FMS1Add BLAST508

Proteomic databases

MaxQBiP50264.
PRIDEiP50264.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Helixi18 – 29Combined sources12
Beta strandi34 – 38Combined sources5
Beta strandi40 – 45Combined sources6
Beta strandi50 – 52Combined sources3
Helixi54 – 56Combined sources3
Beta strandi58 – 62Combined sources5
Turni69 – 71Combined sources3
Helixi73 – 85Combined sources13
Beta strandi90 – 92Combined sources3
Beta strandi98 – 101Combined sources4
Turni102 – 104Combined sources3
Turni111 – 113Combined sources3
Helixi115 – 129Combined sources15
Turni131 – 134Combined sources4
Helixi141 – 152Combined sources12
Helixi153 – 155Combined sources3
Helixi158 – 168Combined sources11
Helixi169 – 171Combined sources3
Helixi172 – 175Combined sources4
Turni179 – 181Combined sources3
Helixi184 – 187Combined sources4
Beta strandi196 – 199Combined sources4
Helixi201 – 209Combined sources9
Helixi214 – 216Combined sources3
Beta strandi217 – 220Combined sources4
Beta strandi223 – 228Combined sources6
Beta strandi230 – 232Combined sources3
Beta strandi234 – 238Combined sources5
Beta strandi243 – 251Combined sources9
Helixi255 – 259Combined sources5
Helixi260 – 262Combined sources3
Beta strandi263 – 265Combined sources3
Beta strandi268 – 270Combined sources3
Beta strandi273 – 276Combined sources4
Helixi280 – 285Combined sources6
Helixi286 – 288Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi295 – 303Combined sources9
Beta strandi311 – 315Combined sources5
Helixi321 – 329Combined sources9
Helixi333 – 339Combined sources7
Helixi353 – 355Combined sources3
Beta strandi358 – 362Combined sources5
Helixi363 – 366Combined sources4
Beta strandi370 – 376Combined sources7
Helixi380 – 386Combined sources7
Turni387 – 389Combined sources3
Helixi391 – 408Combined sources18
Helixi420 – 422Combined sources3
Helixi424 – 426Combined sources3
Beta strandi427 – 429Combined sources3
Beta strandi431 – 437Combined sources7
Turni440 – 442Combined sources3
Turni444 – 448Combined sources5
Helixi461 – 468Combined sources8
Beta strandi470 – 476Combined sources7
Helixi479 – 481Combined sources3
Turni484 – 487Combined sources4
Helixi489 – 508Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50264.

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Phylogenomic databases

HOGENOMiHOG000246632.
InParanoidiP50264.
KOiK13367.
OrthoDBiEOG092C1HE9.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP50264.
PRIDEiP50264.

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.
OrthoDBiEOG092C1HE9.

Enzyme and pathway databases

BioCyciMetaCyc:YMR020W-MONOMER.
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...

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: November 2, 2016
This is version 132 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.