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Database: UniProt
Entry: H2EI28_SOLTU
LinkDB: H2EI28_SOLTU
Original site: H2EI28_SOLTU 
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
//
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