C79A2_ARATH
ID C79A2_ARATH Reviewed; 529 AA.
AC Q9FLC8; F4JZ93; Q9M4Y7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Phenylalanine N-monooxygenase;
DE EC=1.14.14.40 {ECO:0000269|PubMed:10799553};
DE AltName: Full=Cytochrome P450 79A2;
DE AltName: Full=Phenylalanine N-hydroxylase;
GN Name=CYP79A2; OrderedLocusNames=At5g05260; ORFNames=K18I23.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Wassilewskija; TISSUE=Silique;
RX PubMed=10799553; DOI=10.1074/jbc.275.19.14659;
RA Wittstock U., Halkier B.A.;
RT "Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. catalyzes the
RT conversion of L-phenylalanine to phenylacetaldoxime in the biosynthesis of
RT benzylglucosinolate.";
RL J. Biol. Chem. 275:14659-14666(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Converts L-phenylalanine into phenylacetaldoxime, the
CC precursor of benzylglucosinolate (glucotropeolin).
CC {ECO:0000269|PubMed:10799553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = (E)-phenylacetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:33263,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:47793, ChEBI:CHEBI:57618, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58210; EC=1.14.14.40;
CC Evidence={ECO:0000269|PubMed:10799553};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 uM for phenylalanine {ECO:0000269|PubMed:10799553};
CC Vmax=16.6 pmol/min/mg enzyme {ECO:0000269|PubMed:10799553};
CC -!- PATHWAY: Secondary metabolite biosynthesis; phenylglucosinolate
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70255.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF245302; AAF70255.1; ALT_INIT; mRNA.
DR EMBL; AB010692; BAB09969.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70027.1; -; Genomic_DNA.
DR RefSeq; NP_568153.2; NM_120608.2.
DR AlphaFoldDB; Q9FLC8; -.
DR SMR; Q9FLC8; -.
DR STRING; 3702.AT5G05260.1; -.
DR PaxDb; Q9FLC8; -.
DR PRIDE; Q9FLC8; -.
DR EnsemblPlants; AT5G05260.2; AT5G05260.2; AT5G05260.
DR GeneID; 830408; -.
DR Gramene; AT5G05260.2; AT5G05260.2; AT5G05260.
DR KEGG; ath:AT5G05260; -.
DR Araport; AT5G05260; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9FLC8; -.
DR OMA; ENDLFMA; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9FLC8; -.
DR BioCyc; ARA:AT5G05260-MON; -.
DR BioCyc; MetaCyc:AT5G05260-MON; -.
DR BRENDA; 1.14.14.40; 399.
DR SABIO-RK; Q9FLC8; -.
DR UniPathway; UPA00742; -.
DR PRO; PR:Q9FLC8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLC8; baseline and differential.
DR Genevisible; Q9FLC8; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102684; F:L-phenylalanine N-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
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; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..529
FT /note="Phenylalanine N-monooxygenase"
FT /id="PRO_0000052153"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 467
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 529 AA; 59812 MW; D354C991A102FBD8 CRC64;
MLDSTPMLAF IIGLLLLALT MKRKEKKKTM LISPTRNLSL PPGPKSWPLI GNLPEILGRN
KPVFRWIHSL MKELNTDIAC IRLANTHVIP VTSPRIAREI LKKQDSVFAT RPLTMGTEYC
SRGYLTVAVE PQGEQWKKMR RVVASHVTSK KSFQMMLQKR TEEADNLVRY INNRSVKNRG
NAFVVIDLRL AVRQYSGNVA RKMMFGIRHF GKGSEDGSGP GLEEIEHVES LFTVLTHLYA
FALSDYVPWL RFLDLEGHEK VVSNAMRNVS KYNDPFVDER LMQWRNGKMK EPQDFLDMFI
IAKDTDGKPT LSDEEIKAQV TELMLATVDN PSNAAEWGMA EMINEPSIMQ KAVEEIDRVV
GKDRLVIESD LPNLNYVKAC VKEAFRLHPV APFNLPHMST TDTVVDGYFI PKGSHVLISR
MGIGRNPSVW DKPHKFDPER HLSTNTCVDL NESDLNIISF SAGRRGCMGV DIGSAMTYML
LARLIQGFTW LPVPGKNKID ISESKNDLFM AKPLYAVATP RLAPHVYPT
