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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 18FADSequence analysis6
Nucleotide bindingi219 – 224NADPBy similarity6

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003146531 – 447Thiol-specific monooxygenaseAdd BLAST447

Proteomic databases

MaxQBiQ9HFE4.
PRIDEiQ9HFE4.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi277742. 8 interactors.
MINTiMINT-4703048.

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Helixi16 – 26Combined sources11
Turni27 – 29Combined sources3
Beta strandi32 – 37Combined sources6
Beta strandi39 – 44Combined sources6
Helixi45 – 47Combined sources3
Beta strandi59 – 61Combined sources3
Beta strandi71 – 73Combined sources3
Beta strandi74 – 76Combined sources3
Helixi94 – 97Combined sources4
Helixi114 – 125Combined sources12
Helixi126 – 131Combined sources6
Beta strandi135 – 144Combined sources10
Beta strandi147 – 156Combined sources10
Beta strandi161 – 171Combined sources11
Beta strandi175 – 179Combined sources5
Helixi187 – 193Combined sources7
Beta strandi197 – 200Combined sources4
Helixi201 – 203Combined sources3
Helixi207 – 210Combined sources4
Beta strandi215 – 218Combined sources4
Helixi222 – 231Combined sources10
Turni232 – 234Combined sources3
Beta strandi237 – 242Combined sources6
Beta strandi252 – 257Combined sources6
Beta strandi260 – 264Combined sources5
Turni265 – 268Combined sources4
Beta strandi269 – 272Combined sources4
Turni273 – 275Combined sources3
Beta strandi276 – 278Combined sources3
Beta strandi282 – 286Combined sources5
Helixi297 – 300Combined sources4
Turni305 – 307Combined sources3
Beta strandi311 – 315Combined sources5
Beta strandi318 – 320Combined sources3
Turni321 – 323Combined sources3
Beta strandi331 – 335Combined sources5
Beta strandi338 – 340Combined sources3
Helixi342 – 357Combined sources16
Helixi366 – 380Combined sources15
Helixi384 – 386Combined sources3
Beta strandi387 – 389Combined sources3
Turni391 – 393Combined sources3
Helixi394 – 407Combined sources14
Helixi424 – 431Combined sources8
Helixi433 – 440Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9HFE4.

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Phylogenomic databases

HOGENOMiHOG000160105.
InParanoidiQ9HFE4.
OMAiERRHEIK.
OrthoDBiEOG092C1YEF.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VQWX-ray2.40A/B2-447[»]
2GV8X-ray2.10A/B1-447[»]
2GVCX-ray2.22A/B/D/E1-447[»]
ProteinModelPortaliQ9HFE4.
SMRiQ9HFE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277742. 8 interactors.
MINTiMINT-4703048.

Proteomic databases

MaxQBiQ9HFE4.
PRIDEiQ9HFE4.

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.
OMAiERRHEIK.
OrthoDBiEOG092C1YEF.
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...

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: November 30, 2016
This is version 104 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.