C71E7_MANES
ID C71E7_MANES Reviewed; 511 AA.
AC Q6XQ14;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=2-methylbutanal oxime monooxygenase;
DE EC=1.14.14.41 {ECO:0000269|PubMed:21045121};
DE AltName: Full=Cytochrome P450 71E7;
GN Name=CYP71E7; Synonyms=c15;
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], AND TISSUE SPECIFICITY.
RX PubMed=13680228; DOI=10.1007/s00425-003-1098-0;
RA Zhang P., Bohl-Zenger S., Puonti-Kaerlas J., Potrykus I., Gruissem W.;
RT "Two cassava promoters related to vascular expression and storage root
RT formation.";
RL Planta 218:192-203(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=21045121; DOI=10.1104/pp.110.164053;
RA Joergensen K., Morant A.V., Morant M., Jensen N.B., Olsen C.E.,
RA Kannangara R., Motawia M.S., Moeller B.L., Bak S.;
RT "Biosynthesis of the cyanogenic glucosides linamarin and lotaustralin in
RT cassava: isolation, biochemical characterization, and expression pattern of
RT CYP71E7, the oxime-metabolizing cytochrome P450 enzyme.";
RL Plant Physiol. 155:282-292(2011).
CC -!- FUNCTION: Catalyzes the conversion of (E)-2-methylpropanal oxime
CC (valox) to 2-hydroxy-2-methylpropanenitrile (acetone cyanohydrin) and
CC of (E)-2-methylbutanal oxime (ilox) to 2-hydroxy-2-methylbutyronitrile.
CC The reaction takes place in three steps. First, the oxime is isomerized
CC to the (Z)- isomer, next the (Z)-isomer is dehydrated to the
CC corresponding nitrile, followed by a C-hydroxylation of the nitrile.
CC Can use both aliphatic and aromatic oximes as substrates.
CC {ECO:0000269|PubMed:21045121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1E,2S)-2-methylbutanal oxime + O2 + reduced [NADPH--
CC hemoprotein reductase] = 2-hydroxy-2-methylbutanenitrile + H(+) + 2
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:28422,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60954, ChEBI:CHEBI:134628;
CC EC=1.14.14.41; Evidence={ECO:0000269|PubMed:21045121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-2-methylpropanal oxime + O2 + reduced [NADPH--hemoprotein
CC reductase] = 2-hydroxy-2-methylpropanenitrile + H(+) + 2 H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51952,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15348,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61143;
CC EC=1.14.14.41; Evidence={ECO:0000269|PubMed:21045121};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for (Z)-2-methylbutanal oxime {ECO:0000269|PubMed:21045121};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in storage roots, primary roots, petioles
CC and vascular tissues. Expressed in the outer cortex cells, the
CC endodermis and around the xylem, phloem cells and laticifers.
CC {ECO:0000269|PubMed:13680228, ECO:0000269|PubMed:21045121}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY217351; AAP57704.1; -; mRNA.
DR AlphaFoldDB; Q6XQ14; -.
DR SMR; Q6XQ14; -.
DR STRING; 3983.cassava4.1_005817m; -.
DR PRIDE; Q6XQ14; -.
DR KEGG; ag:AAP57704; -.
DR BioCyc; MetaCyc:MON-16012; -.
DR BRENDA; 1.14.14.41; 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; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 PRINTS; PR00385; P450.
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..511
FT /note="2-methylbutanal oxime monooxygenase"
FT /id="PRO_0000407326"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 451
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 511 AA; 58578 MW; 7264BE4BDEE9FC57 CRC64;
MSVAILTSLP PQWLSILAVF LLPILTLLLF RGKDDNQKKG LKLPPGPRQL PLIGNLHQLG
GQPYVDFWKM AKKYGPVMYL QLGRCPTVVL SSTETSKELM KDRDVECCSR PLSVGPGQLS
YNFLDVAFSP YSDYWREMRK LFIFELLSMR RVQTFWYARE EQMDKMIEIL DGAYPNPVNL
TEKVFNMMDG IIGTIAFGRT TYAQQEFRDG FVKVLAATMD MLDNFHAENF FPVVGRFIDS
LTGALAKRQR TFTDVDRYFE KVIEQHLDPN RPKPETEDIV DVLIGLMKDE STSFKITKDH
VKAILMNVFV GGIDTSAVTI TWAFSELLKN PKLMKKAQEE VRRAVGPNKR RVEGKEVEKI
KYIDCIVKET FRKHPPVPLL VPHFSMKHCK IGGYDILPGT TIYVNAWAMG KDPTIWENPE
EYNPDRFMNS EVDFRGSDFE LVPFGAGRRI CPGLAMGTTA VKYILSNLLY GWDYEMPRGK
KFEDFPLIEE GGLTVHNKQD IMVIPKKHKW D
