C79D1_MANES
ID C79D1_MANES Reviewed; 542 AA.
AC Q9M7B8; Q5MD53;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Valine N-monooxygenase 1;
DE EC=1.14.14.38 {ECO:0000269|PubMed:10636899};
DE AltName: Full=Cytochrome P450 79D1;
GN Name=CYP79D1;
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], PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Involved in the biosynthesis of the cyanogenic glucosides
CC linamarin and lotaustralin. Can use L-valine or L-isoleucine as
CC substrate, but not L-leucine, L-phenylalanine, L-tyrosine, D-valine or
CC D-isoleucine. {ECO:0000269|PubMed:10636899,
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 -!- ACTIVITY REGULATION: Inhibited by tetcyclasis but not by 1-
CC aminobenzotriazole (ABT).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for valine {ECO:0000269|PubMed:10636899};
CC KM=1.3 mM for isoleucine {ECO:0000269|PubMed:10636899};
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; AF140613; AAF27289.1; -; mRNA.
DR EMBL; AY834391; AAV97889.1; -; mRNA.
DR AlphaFoldDB; Q9M7B8; -.
DR SMR; Q9M7B8; -.
DR STRING; 3983.cassava4.1_005059m; -.
DR EnsemblPlants; OAY33415; OAY33415; MANES_13G094200.
DR Gramene; OAY33415; OAY33415; MANES_13G094200.
DR KEGG; ag:AAF27289; -.
DR KEGG; ag:AAV97889; -.
DR OMA; DEPLKYK; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.38; 3175.
DR BRENDA; 1.14.14.39; 3175.
DR SABIO-RK; Q9M7B8; -.
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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..542
FT /note="Valine N-monooxygenase 1"
FT /id="PRO_0000407322"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 478
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 30
FT /note="F -> C (in Ref. 2; AAV97889)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="N -> T (in Ref. 2; AAV97889)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="P -> T (in Ref. 2; AAV97889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 61244 MW; E2C7EFFD15CE65B0 CRC64;
MAMNVSTTIG LLNATSFASS SSINTVKILF VTLFISIVST IVKLQKSAAN KEGSKKLPLP
PGPTPWPLIG NIPEMIRYRP TFRWIHQLMK DMNTDICLIR FGRTNFVPIS CPVLAREILK
KNDAIFSNRP KTLSAKSMSG GYLTTIVVPY NDQWKKMRKI LTSEIISPAR HKWLHDKRAE
EADNLVFYIH NQFKANKNVN LRTATRHYGG NVIRKMVFSK RYFGKGMPDG GPGPEEIEHI
DAVFTALKYL YGFCISDFLP FLLGLDLDGQ EKFVLDANKT IRDYQNPLID ERIQQWKSGE
RKEMEDLLDV FITLKDSDGN PLLTPDEIKN QIAEIMIATV DNPSNAIEWA MGEMLNQPEI
LKKATEELDR VVGKDRLVQE SDIPNLDYVK ACAREAFRLH PVAHFNVPHV AMEDTVIGDY
FIPKGSWAVL SRYGLGRNPK TWSDPLKYDP ERHMNEGEVV LTEHELRFVT FSTGRRGCVA
SLLGSCMTTM LLARMLQCFT WTPPANVSKI DLAETLDELT PATPISAFAK PRLAPHLYPT
SP
