ID A0A0N4Z0S2_PARTI Unreviewed; 1238 AA.
AC A0A0N4Z0S2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000030200.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000030200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU361177};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004524}.
CC -!- SIMILARITY: Belongs to the ACDP family.
CC {ECO:0000256|ARBA:ARBA00010484}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183,
CC ECO:0000256|RuleBase:RU361177}.
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DR AlphaFoldDB; A0A0N4Z0S2; -.
DR STRING; 131310.A0A0N4Z0S2; -.
DR WBParaSite; PTRK_0000030200.1; PTRK_0000030200.1; PTRK_0000030200.
DR Proteomes; UP000038045; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum 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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:UniProt.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1905941; P:positive regulation of gonad development; IEA:UniProt.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
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 InterPro; IPR044751; Ion_transp-like_CBS.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF166; DIMETHYLANILINE MONOOXYGENASE [N-OXIDE-FORMING]; 1.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01125; FMOXYGENASE5.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU361177}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 163..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..337
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 423..490
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 1238 AA; 140564 MW; 1A0656A5994B0B04 CRC64;
MVIITSQIPS NISINFGQSE DVRSHSLRSI RDSEIQISGI RLEPLEDEDS PIKGYSKQGI
ALVIPKKDVK VVVFGINLDK IDKIGFTRLT DCTKVLKIIP ITEFKHSTPQ KIDFETNFGY
KNTLFKLCYH KKEDEAKKTF TLVTERDTFI STEIPPRVYI LPFWIQIFMI ILFIFLSGLF
SGLNLGLMSL TPQELELIYK SGSDQEKKYA EAIIPIRKSG NLLLCSLLIG NVIINCSISI
LFDDLTTGII ALIASSSVIV VFGEIFPQSL CVKKGLAVGA RTIWITRFFM ILTFPIAYPI
SKILDWVIGV EVTSYDRKKL MELIKLTTRN ETGLAEELKI AVGAMEIADK TVKDVMTKID
DVFMLPETTI LNAKTVTEIV NMGYTRIPIY AKTRNNVVSL LFIKDLALMD PDDNFTVKTV
CAYNEHVLRF VSEDTPLKTM LEEFKKGDYH LAMVYKKKKS KGKDNFTDLC GLVTLEDIVE
EILQAEIVDE TDVITDNVHK TRRRMKNMKY LSHCFHESSD IPEVISLQLQ MATVQFLSSF
HPIFNSSRIS QHILSKLIKH NVQKIDLTTI HDPNLLKAPS TKTKLYIAGE KSDRFILILE
GRVSVTLGKS SMTFEASPWH PFGTEILDQL LTICPVITEV VNPLNSDRKS KIFFTPDYTC
SVIDKCTYLE LTAPSYIIGY KTSLLQREVE VSPLKLTPRV VTPKKSTPKV MVKVCVVGAG
ASGLPAIKCA LENKFEVVCY EKSNEIGGLW RFKPYPCPDE GTVMRSTVIN TSKEMTAYSD
FPPPAEVANF MHNSELLKYF KSYADHFNLI KHIQFSTAVI NIERHEKFEH NGKWKVTTKN
IVTDEVEENV FDSVMLCTGH HTTPYWPEKF VGQDSFKGKI IHSHDYKDFQ EFVDKKVVVI
GIGNSGGDIA VELSKCAKNV YLSTRSGTWV INRVFDQGEP SDQVYLNRFN YHLRKFLPSS
IENSVLERKV NQRFDHGRFG LKPKHRFLGA HVTVNDELPN RIISGTVIIK SNISSFGDND
VHFDDDTSVE DVDVVIFATG FSFSFPIVEK GTLIDVKDNV VELYKFMYLP TLVPHNTLTI
IGLIQPTGSI MPISEMQCRV HCANLSGNIK LPSKSEMIKD AIRYNEKNMK TFVKSRRHTI
QVHYVEYMEE LAELLKVKPK LLKYLFSDLK LFKTLYFHGL FPYQYRLNGI GAWSGARDAI
IGAEERTFNC TRTRKTPETM KSKPICKVHI CRIACFCD
//