ID G2LIS9_CHLTF Unreviewed; 450 AA.
AC G2LIS9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Flavin-containing monooxygenase 5 {ECO:0000256|ARBA:ARBA00019213};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
DE AltName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 5 {ECO:0000256|ARBA:ARBA00033301};
DE AltName: Full=Dimethylaniline oxidase 5 {ECO:0000256|ARBA:ARBA00029728};
DE AltName: Full=NADPH oxidase {ECO:0000256|ARBA:ARBA00033213};
GN OrderedLocusNames=Cabther_A1547 {ECO:0000313|EMBL:AEP12297.1};
OS Chloracidobacterium thermophilum (strain B).
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP12297.1, ECO:0000313|Proteomes:UP000006791};
RN [1] {ECO:0000313|EMBL:AEP12297.1, ECO:0000313|Proteomes:UP000006791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:AEP12297.1,
RC ECO:0000313|Proteomes:UP000006791};
RX PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA Bryant D.A.;
RT "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL Environ. Microbiol. 14:177-190(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-
CC dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+);
CC Xref=Rhea:RHEA:54860, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16980, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:138375;
CC Evidence={ECO:0000256|ARBA:ARBA00023916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54861;
CC Evidence={ECO:0000256|ARBA:ARBA00023916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octan-3-one = H2O + NADP(+) + pentyl
CC propanoate; Xref=Rhea:RHEA:54840, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:80946, ChEBI:CHEBI:87373;
CC Evidence={ECO:0000256|ARBA:ARBA00001029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54841;
CC Evidence={ECO:0000256|ARBA:ARBA00001029};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octan-3-one = ethyl hexanoate + H2O +
CC NADP(+); Xref=Rhea:RHEA:54856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:80946, ChEBI:CHEBI:86055;
CC Evidence={ECO:0000256|ARBA:ARBA00001105};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54857;
CC Evidence={ECO:0000256|ARBA:ARBA00001105};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + sulcatone = 4-methylpent-3-en-1-yl acetate
CC + H2O + NADP(+); Xref=Rhea:RHEA:54864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16310,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138373;
CC Evidence={ECO:0000256|ARBA:ARBA00000299};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54865;
CC Evidence={ECO:0000256|ARBA:ARBA00000299};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000458};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11261;
CC Evidence={ECO:0000256|ARBA:ARBA00000458};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptan-2-one + NADPH + O2 = H2O + NADP(+) + pentyl
CC acetate; Xref=Rhea:RHEA:54836, ChEBI:CHEBI:5672, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87362;
CC Evidence={ECO:0000256|ARBA:ARBA00000019};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54837;
CC Evidence={ECO:0000256|ARBA:ARBA00000019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptan-4-one + NADPH + O2 = H2O + NADP(+) + propyl
CC butanoate; Xref=Rhea:RHEA:54852, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:89484, ChEBI:CHEBI:89719;
CC Evidence={ECO:0000256|ARBA:ARBA00001839};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54853;
CC Evidence={ECO:0000256|ARBA:ARBA00001839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexan-3-one + NADPH + O2 = H2O + NADP(+) + propyl
CC propanoate; Xref=Rhea:RHEA:54848, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:89828, ChEBI:CHEBI:89891;
CC Evidence={ECO:0000256|ARBA:ARBA00000279};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54849;
CC Evidence={ECO:0000256|ARBA:ARBA00000279};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexan-3-one + NADPH + O2 = ethyl butanoate + H2O +
CC NADP(+); Xref=Rhea:RHEA:54844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:88764, ChEBI:CHEBI:89891;
CC Evidence={ECO:0000256|ARBA:ARBA00000531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54845;
CC Evidence={ECO:0000256|ARBA:ARBA00000531};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004524}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; CP002514; AEP12297.1; -; Genomic_DNA.
DR RefSeq; WP_014100034.1; NC_016024.1.
DR AlphaFoldDB; G2LIS9; -.
DR STRING; 981222.Cabther_A1547; -.
DR KEGG; ctm:Cabther_A1547; -.
DR HOGENOM; CLU_006909_8_3_0; -.
DR OrthoDB; 9778740at2; -.
DR Proteomes; UP000006791; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0047822; F:hypotaurine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002257; Flavin_mOase_5.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01125; FMOXYGENASE5.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006791}.
FT REGION 429..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 51845 MW; 051C56457C0FBEBF CRC64;
MARTGSELPK VCIIGAGCSG ITAAKALHEH QFDFDCYEKS DRVGGNWVFG NKNGMSSAYR
RLFINTSRER MQYSDFPMPK HYPVFPHHSQ IAEYFDAYVD HFGFRSRIRF ETGVKWAERR
DDGVWVITLD NGQVEHYDAL IVANGHHWDP RYPEPPFPGE FDGLILHSHY YVDNDIFRDK
NVVVLGMGNS AMDIACEASE VAKRTYLAAR RGAYIIPKYI FGRPLDQIVT TAKIPWPVRQ
RLFEWTLRLA VGRMEDYGLP KPDHRFGEAH PTISGRILDR LTHGVITPKP NIAELLGNQV
RFADGSVEDV DVIVYCTGYK VTFPFFDENF ISAPDNDLPL FRRVFKPDIP NVFFIGLLQP
LGAIMPLAEA QGQWVASYLK GEYALPPREE MERDMERERA RMFARYVKSK RHTMQVDFDD
YLADLKRERR KGEARARRQG YTLPIPRQVP
//
