ID   C79D2_MANES             Reviewed;         541 AA.
AC   Q9M7B7; Q5MD54;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Valine N-monooxygenase 2;
DE            EC=1.14.14.38 {ECO:0000269|PubMed:10636899};
DE   AltName: Full=Cytochrome P450 79D2;
GN   Name=CYP79D2;
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10636899; DOI=10.1074/jbc.275.3.1966;
RA   Andersen M.D., Busk P.K., Svendsen I., Moller B.L.;
RT   "Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the
RT   first steps in the biosynthesis of the cyanogenic glucosides linamarin and
RT   lotaustralin. Cloning, functional expression in Pichia pastoris, and
RT   substrate specificity of the isolated recombinant enzymes.";
RL   J. Biol. Chem. 275:1966-1975(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16126856; DOI=10.1104/pp.105.065904;
RA   Jorgensen K., Bak S., Busk P.K., Sorensen C., Olsen C.E.,
RA   Puonti-Kaerlas J., Moller B.L.;
RT   "Cassava plants with a depleted cyanogenic glucoside content in leaves and
RT   tubers. Distribution of cyanogenic glucosides, their site of synthesis and
RT   transport, and blockage of the biosynthesis by RNA interference
RT   technology.";
RL   Plant Physiol. 139:363-374(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=15630626; DOI=10.1007/s11103-004-3415-9;
RA   Siritunga D., Sayre R.;
RT   "Engineering cyanogen synthesis and turnover in cassava (Manihot
RT   esculenta).";
RL   Plant Mol. Biol. 56:661-669(2004).
RN   [4]
RP   FUNCTION.
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. Can use L-valine or L-isoleucine as
CC       substrate. {ECO:0000269|PubMed:10636899, ECO:0000269|PubMed:15122013,
CC       ECO:0000269|PubMed:15630626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-valine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] =
CC         (E)-2-methylpropanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:28606, 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:57762, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:61143; EC=1.14.14.38;
CC         Evidence={ECO:0000269|PubMed:10636899};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the epidermis, the next two cortex
CC       cell layers, the endodermis and the pericycle of leaf petioles. Strong
CC       expression around the laticifers among the phloem cells and in
CC       parenchymatic cells between the protoxylem and the metaxylem cells. In
CC       the leaves, preferentially expressed in the mesophyll cells adjacent to
CC       the epidermis. {ECO:0000269|PubMed:16126856}.
CC   -!- MISCELLANEOUS: The synthesis of cyanogenic glucosides is mainly in the
CC       top of the plant and then cyanogenic glucosides are transported
CC       basipetal in the plant to the tuber.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF140614; AAF27290.1; -; mRNA.
DR   EMBL; AY834390; AAV97888.1; -; mRNA.
DR   AlphaFoldDB; Q9M7B7; -.
DR   SMR; Q9M7B7; -.
DR   STRING; 3983.cassava4.1_005079m; -.
DR   EnsemblPlants; OAY35824; OAY35824; MANES_12G133500.
DR   Gramene; OAY35824; OAY35824; MANES_12G133500.
DR   KEGG; ag:AAF27290; -.
DR   KEGG; ag:AAV97888; -.
DR   OMA; TAITVMM; -.
DR   OrthoDB; 702827at2759; -.
DR   BRENDA; 1.14.14.38; 3175.
DR   BRENDA; 1.14.14.39; 3175.
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:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0102002; F:valine N-monooxygenase (oxime forming) activity; IEA:UniProtKB-EC.
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; IPR017972; Cyt_P450_CS.
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.
DR   PROSITE; PS00086; CYTOCHROME_P450; 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..541
FT                   /note="Valine N-monooxygenase 2"
FT                   /id="PRO_0000407323"
FT   TRANSMEM        19..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         477
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"
FT   CONFLICT        508
FT                   /note="R -> K (in Ref. 2; AAV97888)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="A -> S (in Ref. 2; AAV97888)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   541 AA;  61293 MW;  3E17D835E4283395 CRC64;
     MAMNVSTTAT TTASFASTSS MNNTAKILLI TLFISIVSTV IKLQKRASYK KASKNFPLPP
     GPTPWPLIGN IPEMIRYRPT FRWIHQLMKD MNTDICLIRF GKTNVVPISC PVIAREILKK
     HDAVFSNRPK ILCAKTMSGG YLTTIVVPYN DQWKKMRKVL TSEIISPARH KWLHDKRAEE
     ADQLVFYINN QYKSNKNVNV RIAARHYGGN VIRKMMFSKR YFGKGMPDGG PGPEEIMHVD
     AIFTALKYLY GFCISDYLPF LEGLDLDGQE KIVLNANKTI RDLQNPLIEE RIQQWRSGER
     KEMEDLLDVF ITLQDSDGKP LLNPDEIKNQ IAEIMIATID NPANAVEWAM GELINQPELL
     AKATEELDRV VGKDRLVQES DIPNLNYVKA CAREAFRLHP VAYFNVPHVA MEDAVIGDYF
     IPKGSWAILS RYGLGRNPKT WPDPLKYDPE RHLNEGEVVL TEHDLRFVTF STGRRGCVAA
     LLGTTMITMM LARMLQCFTW TPPPNVTRID LSENIDELTP ATPITGFAKP RLAPHLYPTS
     P