ID   C79D4_LOTJA             Reviewed;         536 AA.
AC   Q6J540;
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 2;
DE            EC=1.14.14.39 {ECO:0000269|PubMed:15122013};
DE   AltName: Full=Cytochrome P450 79D4;
GN   Name=CYP79D4;
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=0.7 mM for isoleucine {ECO:0000269|PubMed:15122013};
CC         KM=1.7 mM for leucine {ECO:0000269|PubMed:15122013};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Exclusively detected in 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; AY599896; AAT11921.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6J540; -.
DR   SMR; Q6J540; -.
DR   KEGG; ag:AAT11921; -.
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..536
FT                   /note="Isoleucine N-monooxygenase 2"
FT                   /id="PRO_0000407325"
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   536 AA;  61213 MW;  BE5EF3C7B71928B0 CRC64;
     MGLTPDFLSF CLEFSWTFLL VVIFFFIIFK VTKSHSVNKS KKYKLPPGPK PWPIVGNLPE
     MLANRPATIW IHKLMKEMNT EIACIRLANT IVIPVTCPTI ACEFLKKHDA SFASRPKIMS
     TDIASDGFLT TVLVPYGEQW KKMKRVLVNN LLSPQKHQWL LGKRNEEADN LMFYIYNKCC
     KDVNDGPGLV NIRIAAQHYG GNVFRKLIFN TRYFGKVMED GGPGFEEVEH INATFTILKY
     VYAFSISDFI PFLRRLDLDG HRSKIMKAMG IMKKYHDPII HDRIKQWNDG LKTVEEDLLD
     VLIKLKDASN KPLLTLKEIK AQITELAIEM VDNPSNAFEW ALAEMLNQPE LLKRATEELD
     NVVGKERLVQ ESDIPKLQFV KACAREALRL HPMEYFNVPH LCMNDTMVGD YLFPKGTQVL
     LSRVALGRNP KFWTDPLKFN PERHLKEGID VVLTEPDLRF ISFTTGRRSC PGVTLGTTMT
     IMLFARMLHG FSWSAPPNVS SIDLTQSSDD LFMAKPLCVV AKPRLAAELY STNEFK