ID   C79D3_LOTJA             Reviewed;         535 AA.
AC   Q6J541;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Isoleucine N-monooxygenase 1;
DE            EC=1.14.14.39 {ECO:0000269|PubMed:15122013};
DE   AltName: Full=Cytochrome P450 79D3;
GN   Name=CYP79D3;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15122013; DOI=10.1104/pp.103.038059;
RA   Forslund K., Morant M., Jorgensen B., Olsen C.E., Asamizu E., Sato S.,
RA   Tabata S., Bak S.;
RT   "Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the
RT   cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus.";
RL   Plant Physiol. 135:71-84(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of the cyanogenic glucosides
CC       linamarin and lotaustralin and of the nitirle glucosides
CC       rhodiocyanoside A and D. Can use L-isoleucine > L-valine as substrate,
CC       but not L-leucine, L-phenylalanine or L-tyrosine.
CC       {ECO:0000269|PubMed:15122013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-isoleucine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase]
CC         = (1E,2S)-2-methylbutanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:28602, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58045, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:134628; EC=1.14.14.39;
CC         Evidence={ECO:0000269|PubMed:15122013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 mM for isoleucine {ECO:0000269|PubMed:15122013};
CC         KM=2.6 mM for valine {ECO:0000269|PubMed:15122013};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in aerial parts. Highest
CC       expression in the apical leaves. Also detected in the second leaf from
CC       the top and in the stem. Not expressed in older leaves or roots.
CC       {ECO:0000269|PubMed:15122013}.
CC   -!- MISCELLANEOUS: Unlike in cassava, neither cyanogenic glucosides nor
CC       nitrile glucosides seem to be transported over long distances within
CC       the plant.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY599895; AAT11920.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6J541; -.
DR   SMR; Q6J541; -.
DR   KEGG; ag:AAT11920; -.
DR   BRENDA; 1.14.14.38; 3076.
DR   BRENDA; 1.14.14.39; 3076.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0102001; F:isoleucine N-monooxygenase (oxime forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0019756; P:cyanogenic glycoside biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..535
FT                   /note="Isoleucine N-monooxygenase 1"
FT                   /id="PRO_0000407324"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         470
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   535 AA;  61261 MW;  C268DE180CEBD2AD CRC64;
     MGLMPDFLSL CHEFPWTFLL VVIFSFMIFK VTKTHLVNKS KKYKLPPGPK PWPIVGNLPE
     MLANRPATIW IHKLMKEMNT EIACIRLANT IVIPVTCPTI ACEFLKKHDA SFASRPKIMS
     TDIASDGFIT TVLVPYGEQW KKMKRVLVNN LLSPQKHQWL LGKRNEEADN LMFYIYNKCC
     KDVNDGPGLV NIRIAAQHYG GNVFRKLIFN SRYFGKVMED GGPGFEEVEH INATFTILKY
     VYAFSISDFV PFLRRLDLDG HRSKIMKAMR IMRKYHDPII DDRIKQWNDG LKTVEEDLLD
     VLIKLKDANN KPLLTLKELK AQIIELAIEM VDNPSNAFEW ALAEMINQPE LLKRATEELD
     NVVGKERLVQ ESDIPKLQFV KACAREALRL HPMEYFNVPH LCMNDTMVGD YLFPKGTQVL
     LSRVALGRNP KFWTDPLKFN PERHLKEGID VVLTEPDLRF ISFTTGRRSC PGVALGTTMT
     VMLFARMLHG FSWSPPPDVS SIDLVPSKDD LFLAKPLLLV AKPRLAAELY RTNEI