[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s002940050109; PubMed=8660467 [NCBI, ExPASy, EBI, Israel, Japan] Joets J., Pousset D., Marcireau C., Karst F.; "Characterization of the Saccharomyces cerevisiae FMS1 gene related to Candida albicans corticosteroid-binding protein 1."; Curr. Genet. 30:115-120(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[3]	FUNCTION, AND COFACTOR. DOI=10.1016/S0006-291X(03)00416-9; PubMed=12670477 [NCBI, ExPASy, EBI, Israel, Japan] Landry J., Sternglanz R.; "Yeast Fms1 is a FAD-utilizing polyamine oxidase."; Biochem. Biophys. Res. Commun. 303:771-776(2003).
[4]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[5]	FUNCTION. DOI=10.1073/pnas.1835918100; PubMed=14617780 [NCBI, ExPASy, EBI, Israel, Japan] Chattopadhyay M.K., Tabor C.W., Tabor H.; "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."; Proc. Natl. Acad. Sci. U.S.A. 100:13869-13874(2003).

Comments

FUNCTION: Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.
CATALYTIC ACTIVITY: N¹-acetylspermine + O₂ + H₂O = N¹-acetylspermidine + 3-aminopropanal + H₂O₂.
COFACTOR: FAD.
MISCELLANEOUS: Present with 6960 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the flavin monoamine oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X81848; CAA57442.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49211; CAA89122.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S54021; S54021.

RefSeq

NP_013733.1; -.

3D structure databases

PDB

1RSG; X-ray; 1.90 A; A/B=1-508.	[ExPASy / RCSB / EBI]
1XPQ; X-ray; 2.60 A; A/B/C/D=1-508.	[ExPASy / RCSB / EBI]
1YY5; X-ray; 2.30 A; A/B=1-508.	[ExPASy / RCSB / EBI]
1Z6L; X-ray; 2.50 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3BI2; X-ray; 2.30 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3BI4; X-ray; 2.20 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3BI5; X-ray; 2.50 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3BNM; X-ray; 2.20 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3BNU; X-ray; 2.20 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3CN8; X-ray; 2.40 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3CND; X-ray; 2.50 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3CNP; X-ray; 2.50 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3CNS; X-ray; 2.40 A; A/B=1-508.	[ExPASy / RCSB / EBI]
3CNT; X-ray; 2.70 A; A/B=1-508.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RSG; -.
1XPQ; -.
1YY5; -.
1Z6L; -.
3BI2; -.
3BI4; -.
3BI5; -.
3BNM; -.
3BNU; -.
3CN8; -.
3CND; -.
3CNP; -.
3CNS; -.
3CNT; -.

ModBase

P50264.

Protein-protein interaction databases

DIP

DIP:3959N; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13663; -.

Organism-specific databases

YMR020w; -.

S000004622; FMS1.

Gene expression databases

GermOnline

YMR020W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0008131;	Molecular function: amine oxidase activity (inferred from direct assay from SGD).
GO:0015940;	Biological process: pantothenate biosynthetic process (inferred from mutant phenotype from SGD).
GO:0006598;	Biological process: polyamine catabolic process (inferred from genetic interaction from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR002937; Amino_oxidase.
Graphical view of domain structure.

Pfam

PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.

BLOCKS

P50264.

Genome annotation databases

Ensembl

YMR020W; Saccharomyces cerevisiae. [Contig view]

855034; -.

Z71257_GR; YMR020W.

sce:YMR020W; -.

fig|4932.3.peg.4779; -.

Phylogenomic databases

HOGENOM

P50264; -.

Other

P50264; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 508`	`508`	`Polyamine oxidase FMS1.`	`PRO_0000087317`
`STRAND`	`7 14`	`8`
`HELIX`	`18 29`	`12`
`STRAND`	`34 38`	`5`
`STRAND`	`40 45`	`6`
`STRAND`	`50 52`	`3`
`HELIX`	`54 56`	`3`
`STRAND`	`58 62`	`5`
`TURN`	`69 71`	`3`
`HELIX`	`73 85`	`13`
`STRAND`	`98 101`	`4`
`TURN`	`102 104`	`3`
`TURN`	`111 113`	`3`
`HELIX`	`115 129`	`15`
`HELIX`	`141 152`	`12`
`HELIX`	`153 155`	`3`
`HELIX`	`158 168`	`11`
`HELIX`	`169 171`	`3`
`HELIX`	`172 175`	`4`
`TURN`	`179 181`	`3`
`HELIX`	`184 187`	`4`
`STRAND`	`196 199`	`4`
`HELIX`	`201 209`	`9`
`HELIX`	`214 216`	`3`
`STRAND`	`223 228`	`6`
`STRAND`	`234 238`	`5`
`STRAND`	`243 251`	`9`
`HELIX`	`255 259`	`5`
`HELIX`	`260 262`	`3`
`STRAND`	`273 276`	`4`
`HELIX`	`280 285`	`6`
`STRAND`	`295 303`	`9`
`STRAND`	`311 315`	`5`
`HELIX`	`321 329`	`9`
`HELIX`	`333 339`	`7`
`STRAND`	`358 362`	`5`
`HELIX`	`363 366`	`4`
`STRAND`	`370 376`	`7`
`HELIX`	`380 386`	`7`
`TURN`	`387 389`	`3`
`HELIX`	`391 408`	`18`
`STRAND`	`431 437`	`7`
`TURN`	`440 442`	`3`
`TURN`	`444 448`	`5`
`HELIX`	`461 468`	`8`
`STRAND`	`470 476`	`7`

Sequence information

Length: 508 AA [This is the length of the unprocessed precursor]

Molecular weight: 57806 Da [This is the MW of the unprocessed precursor]

CRC64: 8E135295301EB3CF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNTVSPAKKK VIIIGAGIAG LKAASTLHQN GIQDCLVLEA RDRVGGRLQT VTGYQGRKYD 

        70         80         90        100        110        120 
IGASWHHDTL TNPLFLEEAQ LSLNDGRTRF VFDDDNFIYI DEERGRVDHD KELLLEIVDN 

       130        140        150        160        170        180 
EMSKFAELEF HQHLGVSDCS FFQLVMKYLL QRRQFLTNDQ IRYLPQLCRY LELWHGLDWK 

       190        200        210        220        230        240 
LLSAKDTYFG HQGRNAFALN YDSVVQRIAQ SFPQNWLKLS CEVKSITREP SKNVTVNCED 

       250        260        270        280        290        300 
GTVYNADYVI ITVPQSVLNL SVQPEKNLRG RIEFQPPLKP VIQDAFDKIH FGALGKVIFE 

       310        320        330        340        350        360 
FEECCWSNES SKIVTLANST NEFVEIVRNA ENLDELDSML EREDSQKHTS VTCWSQPLFF 

       370        380        390        400        410        420 
VNLSKSTGVA SFMMLMQAPL TNHIESIRED KERLFSFFQP VLNKIMKCLD SEDVIDGMRP 

       430        440        450        460        470        480 
IENIANANKP VLRNIIVSNW TRDPYSRGAY SACFPGDDPV DMVVAMSNGQ DSRIRFAGEH 

       490        500 
TIMDGAGCAY GAWESGRREA TRISDLLK

P50264 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools