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Protein

Thiol-specific monooxygenase

Gene

fmo1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins (By similarity).By similarity

Cofactori

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 186FADSequence analysis
Nucleotide bindingi219 – 2246NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.14.13.8. 5613.
ReactomeiR-SPO-217271. FMO oxidises nucleophiles.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol-specific monooxygenase (EC:1.14.13.-)
Alternative name(s):
Flavin-dependent monooxygenase
Gene namesi
Name:fmo1
ORF Names:SPBP16F5.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP16F5.08c.
PomBaseiSPBP16F5.08c.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Thiol-specific monooxygenasePRO_0000314653Add
BLAST

Proteomic databases

MaxQBiQ9HFE4.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi277742. 8 interactions.
MINTiMINT-4703048.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi16 – 2611Combined sources
Turni27 – 293Combined sources
Beta strandi32 – 376Combined sources
Beta strandi39 – 446Combined sources
Helixi45 – 473Combined sources
Beta strandi59 – 613Combined sources
Beta strandi71 – 733Combined sources
Beta strandi74 – 763Combined sources
Helixi94 – 974Combined sources
Helixi114 – 12512Combined sources
Helixi126 – 1316Combined sources
Beta strandi135 – 14410Combined sources
Beta strandi147 – 15610Combined sources
Beta strandi161 – 17111Combined sources
Beta strandi175 – 1795Combined sources
Helixi187 – 1937Combined sources
Beta strandi197 – 2004Combined sources
Helixi201 – 2033Combined sources
Helixi207 – 2104Combined sources
Beta strandi215 – 2184Combined sources
Helixi222 – 23110Combined sources
Turni232 – 2343Combined sources
Beta strandi237 – 2426Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi260 – 2645Combined sources
Turni265 – 2684Combined sources
Beta strandi269 – 2724Combined sources
Turni273 – 2753Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi282 – 2865Combined sources
Helixi297 – 3004Combined sources
Turni305 – 3073Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi318 – 3203Combined sources
Turni321 – 3233Combined sources
Beta strandi331 – 3355Combined sources
Beta strandi338 – 3403Combined sources
Helixi342 – 35716Combined sources
Helixi366 – 38015Combined sources
Helixi384 – 3863Combined sources
Beta strandi387 – 3893Combined sources
Turni391 – 3933Combined sources
Helixi394 – 40714Combined sources
Helixi424 – 4318Combined sources
Helixi433 – 4408Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VQWX-ray2.40A/B2-447[»]
2GV8X-ray2.10A/B1-447[»]
2GVCX-ray2.22A/B/D/E1-447[»]
ProteinModelPortaliQ9HFE4.
SMRiQ9HFE4. Positions 3-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HFE4.

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Phylogenomic databases

HOGENOMiHOG000160105.
InParanoidiQ9HFE4.
OMAiREHIAFR.
OrthoDBiEOG7B31X1.
PhylomeDBiQ9HFE4.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
[Graphical view]
PfamiPF00743. FMO-like. 2 hits.
[Graphical view]
PRINTSiPR00370. FMOXYGENASE.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9HFE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCLPTIRKIA IIGAGPSGLV TAKALLAEKA FDQVTLFERR GSPGGVWNYT
60 70 80 90 100
STLSNKLPVP STNPILTTEP IVGPAALPVY PSPLYRDLQT NTPIELMGYC
110 120 130 140 150
DQSFKPQTLQ FPHRHTIQEY QRIYAQPLLP FIKLATDVLD IEKKDGSWVV
160 170 180 190 200
TYKGTKAGSP ISKDIFDAVS ICNGHYEVPY IPNIKGLDEY AKAVPGSVLH
210 220 230 240 250
SSLFREPELF VGESVLVVGG ASSANDLVRH LTPVAKHPIY QSLLGGGDIQ
260 270 280 290 300
NESLQQVPEI TKFDPTTREI YLKGGKVLSN IDRVIYCTGY LYSVPFPSLA
310 320 330 340 350
KLKSPETKLI DDGSHVHNVY QHIFYIPDPT LAFVGLALHV VPFPTSQAQA
360 370 380 390 400
AFLARVWSGR LKLPSKEEQL KWQDELMFSL SGANNMYHSL DYPKDATYIN
410 420 430 440
KLHDWCKQAT PVLEEEFPSP YWGEKERSIR ENMWSIRAKF FGIEPPK
Length:447
Mass (Da):49,889
Last modified:March 1, 2001 - v1
Checksum:i4392F5D9791C406F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAC08547.1.
RefSeqiNP_595782.1. NM_001021682.2.

Genome annotation databases

EnsemblFungiiSPBP16F5.08c.1; SPBP16F5.08c.1:pep; SPBP16F5.08c.
GeneIDi2541228.
KEGGispo:SPBP16F5.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAC08547.1.
RefSeqiNP_595782.1. NM_001021682.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VQWX-ray2.40A/B2-447[»]
2GV8X-ray2.10A/B1-447[»]
2GVCX-ray2.22A/B/D/E1-447[»]
ProteinModelPortaliQ9HFE4.
SMRiQ9HFE4. Positions 3-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277742. 8 interactions.
MINTiMINT-4703048.

Proteomic databases

MaxQBiQ9HFE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP16F5.08c.1; SPBP16F5.08c.1:pep; SPBP16F5.08c.
GeneIDi2541228.
KEGGispo:SPBP16F5.08c.

Organism-specific databases

EuPathDBiFungiDB:SPBP16F5.08c.
PomBaseiSPBP16F5.08c.

Phylogenomic databases

HOGENOMiHOG000160105.
InParanoidiQ9HFE4.
OMAiREHIAFR.
OrthoDBiEOG7B31X1.
PhylomeDBiQ9HFE4.

Enzyme and pathway databases

BRENDAi1.14.13.8. 5613.
ReactomeiR-SPO-217271. FMO oxidises nucleophiles.

Miscellaneous databases

EvolutionaryTraceiQ9HFE4.
PROiQ9HFE4.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
[Graphical view]
PfamiPF00743. FMO-like. 2 hits.
[Graphical view]
PRINTSiPR00370. FMOXYGENASE.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-447 IN COMPLEX WITH FAD; NADPH AND METHIMAZOLE.

Entry informationi

Entry nameiFMO1_SCHPO
AccessioniPrimary (citable) accession number: Q9HFE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.