ID H2EI28_SOLTU Unreviewed; 408 AA.
AC H2EI28;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, 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 Solanum tuberosum subsp. andigenum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=80418 {ECO:0000313|EMBL:AEX15600.1};
RN [1] {ECO:0000313|EMBL:AEX15600.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Stolons induced for tuberization {ECO:0000313|EMBL:AEX15600.1};
RX PubMed=22689826; DOI=10.1093/jxb/ers132;
RA Roumeliotis E., Kloosterman B., Oortwijn M., Kohlen W., Bouwmeester H.J.,
RA Visser R.G., Bachem C.W.;
RT "The effects of auxin and strigolactones on tuber initiation and stolon
RT architecture in potato.";
RL J. Exp. Bot. 63:4539-4547(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.168;
CC Evidence={ECO:0000256|ARBA:ARBA00035920};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361177};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004814}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|RuleBase:RU361177}.
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DR EMBL; JN935396; AEX15600.1; -; mRNA.
DR AlphaFoldDB; H2EI28; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:RHEA.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009851; P:auxin biosynthetic 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; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR PANTHER; PTHR43539:SF53; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 2: Evidence at transcript level;
KW Auxin biosynthesis {ECO:0000256|ARBA:ARBA00023070};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177}; Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|RuleBase:RU361177};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 408 AA; 45746 MW; 97F76161C1790688 CRC64;
MVSFNGQDLF SSRCVWVNGP VIVGAGPSGL AVGACLKEQG IPFVILEKSD CIASLWQKKT
YNRLKLHLPK QFCQLPKFPF PQHYPEYPTK KQFIDYLESY ARKFDINPMF NECVQFAKYD
QICKLWRVKT ISPNGLEVEY ICQWLVVATG ENAEKVVPNI EGLKEFGGEV IHACDYKSGE
KFSGKKVLVV GCGNSGMEVS LDLSNHNAHP SLVCRSSVHV LPREIFGKSI FELAMFMMKW
LPLWLVDKIL LILTWFILGN IEKYGLKRPK IGPLELKNTQ GKTPVLDIGA LEKIRSRKIN
VVPGIKKFSC GTVELVNGEK LEIDSVVLAT GYCSNVPFWL KESEFFSKNG FPKAPFPNSW
KGKSGLYAVG FTRRGLSGAS ADAIQIAQDI TKAYNEDIMQ KKQKISTL
//