C79F2_ARATH
ID C79F2_ARATH Reviewed; 537 AA.
AC Q9FUY7; Q94JZ4; Q9SA39;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hexahomomethionine N-hydroxylase;
DE EC=1.14.14.42 {ECO:0000269|Ref.4};
DE AltName: Full=Cytochrome P450 79F2;
GN Name=CYP79F2; OrderedLocusNames=At1g16400; ORFNames=F3O9.20;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-537, CATALYTIC ACTIVITY, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX DOI=10.1046/j.1365-313X.2003.01679.x;
RA Chen S., Glawischnig E., Joergensen K., Naur P., Joergensen B.,
RA Olsen C.-E., Hansen C.H., Rasmussen H., Pickett J.A., Halkier B.A.;
RT "CYP79F1 and CYP79F2 have distinct functions in the biosynthesis of
RT aliphatic glucosinolates in Arabidopsis.";
RL Plant J. 33:923-937(2003).
RN [5]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11226190; DOI=10.2307/3871281;
RA Reintanz B., Lehnen M., Reichelt M., Gershenzon J., Kowalczyk M.,
RA Sandberg G., Godde M., Uhl R., Palme K.;
RT "Bus, a bushy Arabidopsis CYP79F1 knockout mutant with abolished synthesis
RT of short-chain aliphatic glucosinolates.";
RL Plant Cell 13:351-367(2001).
RN [6]
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=12529537; DOI=10.1104/pp.011015;
RA Mikkelsen M.D., Petersen B.L., Glawischnig E., Jensen A.B., Andreasson E.,
RA Halkier B.A.;
RT "Modulation of CYP79 genes and glucosinolate profiles in Arabidopsis by
RT defense signaling pathways.";
RL Plant Physiol. 131:298-308(2003).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15194821; DOI=10.1104/pp.104.040113;
RA Tantikanjana T., Mikkelsen M.D., Hussain M., Halkier B.A., Sundaresan V.;
RT "Functional analysis of the tandem-duplicated P450 genes SPS/BUS/CYP79F1
RT and CYP79F2 in glucosinolate biosynthesis and plant development by Ds
RT transposition-generated double mutants.";
RL Plant Physiol. 135:840-848(2004).
CC -!- FUNCTION: Catalyzes the conversion of the long chain elongated
CC methionines penta- and hexahomomethionine to their corresponding
CC aldoximes 8-methylthiooctanaldoxime and 9-methylthiononanaldoxime.
CC {ECO:0000269|PubMed:15194821, ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-hexahomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = (E)-9-(methylsulfanyl)nonanal oxime + CO2 + 2 H(+) + 3
CC H2O + 2 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:33295, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:134636, ChEBI:CHEBI:134685; EC=1.14.14.42;
CC Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pentahomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = (E)-8-(methylsulfanyl)octanal oxime + CO2 + 2 H(+) + 3
CC H2O + 2 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:33291, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:134635, ChEBI:CHEBI:134684; EC=1.14.14.42;
CC Evidence={ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-polyhomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = an (E)-omega-(methylsulfanyl)-alkanal oxime + CO2 + 2
CC H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:51972, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC Rhea:RHEA-COMP:13111, Rhea:RHEA-COMP:13114, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134631,
CC ChEBI:CHEBI:134680; EC=1.14.14.42; Evidence={ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=374 uM for pentahomomethionine {ECO:0000269|Ref.4};
CC KM=26 uM for hexahomomethionine {ECO:0000269|Ref.4};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11226190}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11226190}.
CC -!- TISSUE SPECIFICITY: Highly expressed in hypocotyl and roots. Lower
CC expression in siliques, stems and leaves. Barely detectable in flowers.
CC Expressed only in the vascular bundles in apical plant parts.
CC {ECO:0000269|PubMed:11226190, ECO:0000269|Ref.4}.
CC -!- DEVELOPMENTAL STAGE: Expressed above the root elongation zone, but not
CC in the root primordium. {ECO:0000269|PubMed:15194821}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12529537}.
CC -!- DISRUPTION PHENOTYPE: Plants show a slight lateral root growth
CC reduction. {ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34692.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006341; AAD34692.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29446.1; -; Genomic_DNA.
DR EMBL; AY064649; AAL47360.1; -; mRNA.
DR EMBL; AF370512; AAK43889.1; -; mRNA.
DR EMBL; AF275259; AAG24796.1; -; mRNA.
DR PIR; C86299; C86299.
DR RefSeq; NP_563995.2; NM_101506.3.
DR AlphaFoldDB; Q9FUY7; -.
DR SMR; Q9FUY7; -.
DR STRING; 3702.AT1G16400.1; -.
DR PaxDb; Q9FUY7; -.
DR PRIDE; Q9FUY7; -.
DR ProteomicsDB; 240582; -.
DR EnsemblPlants; AT1G16400.1; AT1G16400.1; AT1G16400.
DR GeneID; 838210; -.
DR Gramene; AT1G16400.1; AT1G16400.1; AT1G16400.
DR KEGG; ath:AT1G16400; -.
DR Araport; AT1G16400; -.
DR TAIR; locus:2032865; AT1G16400.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9FUY7; -.
DR OMA; FHLAMKE; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9FUY7; -.
DR BioCyc; ARA:AT1G16400-MON; -.
DR BioCyc; MetaCyc:AT1G16400-MON; -.
DR BRENDA; 1.14.14.42; 399.
DR SABIO-RK; Q9FUY7; -.
DR PRO; PR:Q9FUY7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FUY7; baseline and differential.
DR Genevisible; Q9FUY7; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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: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; IDA:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
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..537
FT /note="Hexahomomethionine N-hydroxylase"
FT /id="PRO_0000315844"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 61432 MW; 1808F8A0203F2795 CRC64;
MMMKISFNTC FQILLGFIVF IASITLLGRI FSRPSKTKDR CRQLPPGRPG WPILGNLPEL
IMTRPRSKYF HLAMKELKTD IACFNFAGTH TITINSDEIA REAFRERDAD LADRPQLSIV
ESIGDNYKTM GTSSYGEHFM KMKKVITTEI MSVKTLNMLE AARTIEADNL IAYIHSMYQR
SETVDVRELS RVYGYAVTMR MLFGRRHVTK ENMFSDDGRL GKAEKHHLEV IFNTLNCLPG
FSPVDYVDRW LGGWNIDGEE ERAKVNVNLV RSYNNPIIDE RVEIWREKGG KAAVEDWLDT
FITLKDQNGN YLVTPDEIKA QCVEFCIAAI DNPANNMEWT LGEMLKNPEI LRKALKELDE
VVGKDRLVQE SDIRNLNYLK ACCRETFRIH PSAHYVPPHV ARQDTTLGGY FIPKGSHIHV
CRPGLGRNPK IWKDPLAYEP ERHLQGDGIT KEVTLVETEM RFVSFSTGRR GCVGVKVGTI
MMAMMLARFL QGFNWKLHRD FGPLSLEEDD ASLLMAKPLL LSVEPRLASN LYPKFRP
