C79F1_ARATH
ID C79F1_ARATH Reviewed; 538 AA.
AC Q949U1; A5YZH1; A5YZH3; A5YZH4; A5YZH6; A5YZH9; A5YZI0; A5YZI1; A5YZI6;
AC A5YZI9; A5YZJ1; Q3EDB1; Q941N8; Q9SA40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Dihomomethionine N-hydroxylase;
DE EC=1.14.14.42 {ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033};
DE AltName: Full=Cytochrome P450 79F1;
DE AltName: Full=Protein BUSHY 1;
DE AltName: Full=Protein SUPERSHOOT 1;
DE AltName: Full=Trihomomethionine N-hydroxylase;
GN Name=CYP79F1; Synonyms=BUS1, SPS1; OrderedLocusNames=At1g16410;
GN ORFNames=F3O9.21;
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 [GENOMIC DNA] OF 1-247, AND VARIANTS.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
RC cv. Edi-0, cv. Ga-0, cv. Kas-1, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0,
RC cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0,
RC cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and cv. Wassilewskija;
RX PubMed=17435248; DOI=10.1534/genetics.107.071928;
RA Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
RT "The genetic architecture of shoot branching in Arabidopsis thaliana: a
RT comparative assessment of candidate gene associations vs. quantitative
RT trait locus mapping.";
RL Genetics 176:1223-1236(2007).
RN [5]
RP IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
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 FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=11133994; DOI=10.1074/jbc.m010123200;
RA Hansen C.H., Wittstock U., Olsen C.-E., Hick A.J., Pickett J.A.,
RA Halkier B.A.;
RT "Cytochrome P450 CYP79F1 from Arabidopsis catalyzes the conversion of
RT dihomomethionine and trihomomethionine to the corresponding aldoximes in
RT the biosynthesis of aliphatic glucosinolates.";
RL J. Biol. Chem. 276:11078-11085(2001).
RN [7]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12609033; 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 [8]
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 [9]
RP FUNCTION.
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 short chain elongated
CC methionines di-, tri-, and tetrahomomethionine to their respective
CC aldoximes 5-methylthiopentanaldoxime, 6-methylthiohexanaldoxime, and 7-
CC methylheptanaldoxime. {ECO:0000269|PubMed:11133994,
CC ECO:0000269|PubMed:11226190, ECO:0000269|PubMed:15194821}.
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;
CC Evidence={ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dihomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = (E)-5-(methylsulfanyl)pentanal oxime + CO2 + 2 H(+) + 3
CC H2O + 2 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:32719, 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:134632, ChEBI:CHEBI:134682; EC=1.14.14.42;
CC Evidence={ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-trihomomethionine + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = (E)-6-(methylsulfanyl)hexanal oxime + CO2 + 2 H(+) + 3
CC H2O + 2 oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:32723, 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:134633, ChEBI:CHEBI:134681; EC=1.14.14.42;
CC Evidence={ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for dihomomethionine {ECO:0000269|PubMed:12609033};
CC KM=37 uM for trihomomethionine {ECO:0000269|PubMed:12609033};
CC KM=194 uM for tetrahomomethionine {ECO:0000269|PubMed:12609033};
CC KM=216 uM for pentahomomethionine {ECO:0000269|PubMed:12609033};
CC KM=74 uM for hexahomomethionine {ECO:0000269|PubMed:12609033};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11226190}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11226190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q949U1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q949U1-2; Sequence=VSP_030739, VSP_030740;
CC -!- TISSUE SPECIFICITY: Highly expressed in cotyledons, leaves, stems and
CC siliques. Detected in flowers and lateral roots, but not in the main
CC root. Expressed only in the vascular bundles in apical plant parts.
CC {ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:11226190,
CC ECO:0000269|PubMed:12609033}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12529537}.
CC -!- DISRUPTION PHENOTYPE: Plants have a bushy phenotype with crinkled
CC leaves and retarded vascularization. {ECO:0000269|PubMed:11226190,
CC ECO:0000269|PubMed:12609033}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34693.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006341; AAD34693.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29447.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29448.1; -; Genomic_DNA.
DR EMBL; AY035021; AAK59526.1; -; mRNA.
DR EMBL; AY050890; AAK92827.1; -; mRNA.
DR EMBL; AY114074; AAM45122.1; -; mRNA.
DR EMBL; EF598753; ABR09166.1; -; Genomic_DNA.
DR EMBL; EF598754; ABR09167.1; -; Genomic_DNA.
DR EMBL; EF598755; ABR09168.1; -; Genomic_DNA.
DR EMBL; EF598756; ABR09169.1; -; Genomic_DNA.
DR EMBL; EF598757; ABR09170.1; -; Genomic_DNA.
DR EMBL; EF598758; ABR09171.1; -; Genomic_DNA.
DR EMBL; EF598759; ABR09172.1; -; Genomic_DNA.
DR EMBL; EF598760; ABR09173.1; -; Genomic_DNA.
DR EMBL; EF598761; ABR09174.1; -; Genomic_DNA.
DR EMBL; EF598762; ABR09175.1; -; Genomic_DNA.
DR EMBL; EF598763; ABR09176.1; -; Genomic_DNA.
DR EMBL; EF598764; ABR09177.1; -; Genomic_DNA.
DR EMBL; EF598765; ABR09178.1; -; Genomic_DNA.
DR EMBL; EF598766; ABR09179.1; -; Genomic_DNA.
DR EMBL; EF598767; ABR09180.1; -; Genomic_DNA.
DR EMBL; EF598768; ABR09181.1; -; Genomic_DNA.
DR EMBL; EF598769; ABR09182.1; -; Genomic_DNA.
DR EMBL; EF598770; ABR09183.1; -; Genomic_DNA.
DR EMBL; EF598771; ABR09184.1; -; Genomic_DNA.
DR EMBL; EF598772; ABR09185.1; -; Genomic_DNA.
DR EMBL; EF598773; ABR09186.1; -; Genomic_DNA.
DR EMBL; EF598774; ABR09187.1; -; Genomic_DNA.
DR EMBL; EF598775; ABR09188.1; -; Genomic_DNA.
DR EMBL; EF598776; ABR09189.1; -; Genomic_DNA.
DR PIR; D86299; D86299.
DR RefSeq; NP_563996.2; NM_101507.3. [Q949U1-1]
DR RefSeq; NP_973840.1; NM_202111.2. [Q949U1-2]
DR AlphaFoldDB; Q949U1; -.
DR SMR; Q949U1; -.
DR BioGRID; 23451; 4.
DR IntAct; Q949U1; 3.
DR STRING; 3702.AT1G16410.1; -.
DR PaxDb; Q949U1; -.
DR PRIDE; Q949U1; -.
DR ProteomicsDB; 239120; -. [Q949U1-1]
DR EnsemblPlants; AT1G16410.1; AT1G16410.1; AT1G16410. [Q949U1-1]
DR EnsemblPlants; AT1G16410.2; AT1G16410.2; AT1G16410. [Q949U1-2]
DR GeneID; 838211; -.
DR Gramene; AT1G16410.1; AT1G16410.1; AT1G16410. [Q949U1-1]
DR Gramene; AT1G16410.2; AT1G16410.2; AT1G16410. [Q949U1-2]
DR KEGG; ath:AT1G16410; -.
DR Araport; AT1G16410; -.
DR TAIR; locus:2032890; AT1G16410.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q949U1; -.
DR OMA; PRHKYID; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q949U1; -.
DR BioCyc; ARA:AT1G16410-MON; -.
DR BioCyc; MetaCyc:AT1G16410-MON; -.
DR BRENDA; 1.14.14.42; 399.
DR SABIO-RK; Q949U1; -.
DR PRO; PR:Q949U1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q949U1; baseline and differential.
DR Genevisible; Q949U1; 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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0103096; F:CYP79F1 dihomomethionine monooxygenase activity; IEA:RHEA.
DR GO; GO:0103097; F:CYP79F1 trihomomethionine monooxygenase activity; IEA:RHEA.
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 GO; GO:0009625; P:response to insect; IEP: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 Alternative splicing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Dihomomethionine N-hydroxylase"
FT /id="PRO_0000315843"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 417..423
FT /note="SHIHVCR -> KKKKKKR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030739"
FT VAR_SEQ 424..538
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030740"
FT VARIANT 43
FT /note="C -> R (in strain: cv. Ag-0, cv. Br-0, cv. C24, cv.
FT Ct-1, cv. Edi-0, cv. Kas-1, cv. Kin-0, cv. Landsberg
FT erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1,
FT cv. Nok-3, cv. Oy-0, cv. Sorbo, cv. Van-0, cv. Wa-1 and cv.
FT Wassilewskija)"
FT VARIANT 83
FT /note="A -> G (in strain: cv. Se-0)"
FT VARIANT 120
FT /note="I -> T (in strain: cv. Br-0 and cv. Mt-0)"
FT VARIANT 154
FT /note="V -> F (in strain: cv. Ag-0, cv. Cvi-1, cv. Edi-0,
FT cv. Ll-0 and cv. Nok-3)"
FT VARIANT 158
FT /note="K -> N (in strain: cv. Ag-0, cv. Br-0, cv. Cvi-1,
FT cv. Edi-0, cv. Ll-0, cv. Lz-0, cv. Mt-0, cv. Nok-3 and cv.
FT Van-0)"
FT VARIANT 159
FT /note="M -> I (in strain: cv. Nd-1)"
FT VARIANT 161
FT /note="E -> K (in strain: cv. Lz-0 and cv. Van-0)"
FT VARIANT 192
FT /note="R -> W (in strain: cv. Kin-0)"
FT VARIANT 222
FT /note="G -> V (in strain: cv. Ll-0)"
SQ SEQUENCE 538 AA; 61695 MW; 4001A1179BBE5ADD CRC64;
MMSFTTSLPY PFHILLVFIL SMASITLLGR ILSRPTKTKD RSCQLPPGPP GWPILGNLPE
LFMTRPRSKY FRLAMKELKT DIACFNFAGI RAITINSDEI AREAFRERDA DLADRPQLFI
METIGDNYKS MGISPYGEQF MKMKRVITTE IMSVKTLKML EAARTIEADN LIAYVHSMYQ
RSETVDVREL SRVYGYAVTM RMLFGRRHVT KENVFSDDGR LGNAEKHHLE VIFNTLNCLP
SFSPADYVER WLRGWNVDGQ EKRVTENCNI VRSYNNPIID ERVQLWREEG GKAAVEDWLD
TFITLKDQNG KYLVTPDEIK AQCVEFCIAA IDNPANNMEW TLGEMLKNPE ILRKALKELD
EVVGRDRLVQ ESDIPNLNYL KACCRETFRI HPSAHYVPSH LARQDTTLGG YFIPKGSHIH
VCRPGLGRNP KIWKDPLVYK PERHLQGDGI TKEVTLVETE MRFVSFSTGR RGCIGVKVGT
IMMVMLLARF LQGFNWKLHQ DFGPLSLEED DASLLMAKPL HLSVEPRLAP NLYPKFRP
