FMO1_SCHPO
ID FMO1_SCHPO Reviewed; 447 AA.
AC Q9HFE4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Thiol-specific monooxygenase;
DE EC=1.14.13.-;
DE AltName: Full=Flavin-dependent monooxygenase;
GN Name=fmo1; ORFNames=SPBP16F5.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-447 IN COMPLEX WITH FAD; NADPH
RP AND METHIMAZOLE.
RX PubMed=16777962; DOI=10.1073/pnas.0602398103;
RA Eswaramoorthy S., Bonanno J.B., Burley S.K., Swaminathan S.;
RT "Mechanism of action of a flavin-containing monooxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9832-9837(2006).
CC -!- FUNCTION: Flavin-dependent oxidation of thiol-containing compounds.
CC Probably required for the correct folding of disulfide-bonded proteins
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAC08547.1; -; Genomic_DNA.
DR RefSeq; NP_595782.1; NM_001021682.2.
DR PDB; 1VQW; X-ray; 2.40 A; A/B=2-447.
DR PDB; 2GV8; X-ray; 2.10 A; A/B=1-447.
DR PDB; 2GVC; X-ray; 2.22 A; A/B/D/E=1-447.
DR PDBsum; 1VQW; -.
DR PDBsum; 2GV8; -.
DR PDBsum; 2GVC; -.
DR AlphaFoldDB; Q9HFE4; -.
DR SMR; Q9HFE4; -.
DR BioGRID; 277742; 8.
DR STRING; 4896.SPBP16F5.08c.1; -.
DR iPTMnet; Q9HFE4; -.
DR MaxQB; Q9HFE4; -.
DR PaxDb; Q9HFE4; -.
DR DNASU; 2541228; -.
DR EnsemblFungi; SPBP16F5.08c.1; SPBP16F5.08c.1:pep; SPBP16F5.08c.
DR GeneID; 2541228; -.
DR KEGG; spo:SPBP16F5.08c; -.
DR PomBase; SPBP16F5.08c; fmo1.
DR VEuPathDB; FungiDB:SPBP16F5.08c; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_0_1; -.
DR InParanoid; Q9HFE4; -.
DR OMA; FMEWEHH; -.
DR PhylomeDB; Q9HFE4; -.
DR BRENDA; 1.14.13.8; 5613.
DR EvolutionaryTrace; Q9HFE4; -.
DR PRO; PR:Q9HFE4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISM:PomBase.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; ISM:PomBase.
DR GO; GO:0050661; F:NADP binding; ISM:PomBase.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IC:PomBase.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Thiol-specific monooxygenase"
FT /id="PRO_0000314653"
FT BINDING 13..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8,
FT ECO:0007744|PDB:2GVC"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8,
FT ECO:0007744|PDB:2GVC"
FT BINDING 46..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8,
FT ECO:0007744|PDB:2GVC"
FT BINDING 90..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:2GV8"
FT BINDING 91..92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8,
FT ECO:0007744|PDB:2GVC"
FT BINDING 137..138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8,
FT ECO:0007744|PDB:2GVC"
FT BINDING 223..226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16777962,
FT ECO:0007744|PDB:2GV8"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2GV8"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2GVC"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2GVC"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:2GV8"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2GV8"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2GV8"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:2GV8"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2GV8"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 366..380
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2GV8"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1VQW"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:2GV8"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:2GV8"
SQ SEQUENCE 447 AA; 49889 MW; 4392F5D9791C406F CRC64;
MCLPTIRKIA IIGAGPSGLV TAKALLAEKA FDQVTLFERR GSPGGVWNYT STLSNKLPVP
STNPILTTEP IVGPAALPVY PSPLYRDLQT NTPIELMGYC DQSFKPQTLQ FPHRHTIQEY
QRIYAQPLLP FIKLATDVLD IEKKDGSWVV TYKGTKAGSP ISKDIFDAVS ICNGHYEVPY
IPNIKGLDEY AKAVPGSVLH SSLFREPELF VGESVLVVGG ASSANDLVRH LTPVAKHPIY
QSLLGGGDIQ NESLQQVPEI TKFDPTTREI YLKGGKVLSN IDRVIYCTGY LYSVPFPSLA
KLKSPETKLI DDGSHVHNVY QHIFYIPDPT LAFVGLALHV VPFPTSQAQA AFLARVWSGR
LKLPSKEEQL KWQDELMFSL SGANNMYHSL DYPKDATYIN KLHDWCKQAT PVLEEEFPSP
YWGEKERSIR ENMWSIRAKF FGIEPPK
