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Dihomomethionine N-hydroxylase (EC 1.14.14.42) (Cytochrome P450 79F1) (Protein BUSHY 1) (Protein SUPERSHOOT 1) (Trihomomethionine N-hydroxylase)

 C79F1_ARATH             Reviewed;         538 AA.
Q949U1; A5YZH1; A5YZH3; A5YZH4; A5YZH6; A5YZH9; A5YZI0; A5YZI1;
A5YZI6; A5YZI9; A5YZJ1; Q3EDB1; Q941N8; Q9SA40;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=Dihomomethionine N-hydroxylase;
EC=1.14.14.42 {ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033};
AltName: Full=Cytochrome P450 79F1;
AltName: Full=Protein BUSHY 1;
AltName: Full=Protein SUPERSHOOT 1;
AltName: Full=Trihomomethionine N-hydroxylase;
Name=CYP79F1; Synonyms=BUS1, SPS1; OrderedLocusNames=At1g16410;
ORFNames=F3O9.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-247, AND VARIANTS.
STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
cv. Edi-0, cv. Ga-0, cv. Kas-1, cv. Kin-0, cv. Landsberg erecta,
cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0,
cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and
cv. Wassilewskija;
PubMed=17435248; DOI=10.1534/genetics.107.071928;
Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
"The genetic architecture of shoot branching in Arabidopsis thaliana:
a comparative assessment of candidate gene associations vs.
quantitative trait locus mapping.";
Genetics 176:1223-1236(2007).
[5]
IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=11226190; DOI=10.1105/tpc.13.2.351;
Reintanz B., Lehnen M., Reichelt M., Gershenzon J., Kowalczyk M.,
Sandberg G., Godde M., Uhl R., Palme K.;
"Bus, a bushy Arabidopsis CYP79F1 knockout mutant with abolished
synthesis of short-chain aliphatic glucosinolates.";
Plant Cell 13:351-367(2001).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=11133994; DOI=10.1074/jbc.M010123200;
Hansen C.H., Wittstock U., Olsen C.-E., Hick A.J., Pickett J.A.,
Halkier B.A.;
"Cytochrome P450 CYP79F1 from Arabidopsis catalyzes the conversion of
dihomomethionine and trihomomethionine to the corresponding aldoximes
in the biosynthesis of aliphatic glucosinolates.";
J. Biol. Chem. 276:11078-11085(2001).
[7]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
PubMed=12609033; DOI=10.1046/j.1365-313X.2003.01679.x;
Chen S., Glawischnig E., Joergensen K., Naur P., Joergensen B.,
Olsen C.-E., Hansen C.H., Rasmussen H., Pickett J.A., Halkier B.A.;
"CYP79F1 and CYP79F2 have distinct functions in the biosynthesis of
aliphatic glucosinolates in Arabidopsis.";
Plant J. 33:923-937(2003).
[8]
INDUCTION BY METHYL JASMONATE.
PubMed=12529537; DOI=10.1104/pp.011015;
Mikkelsen M.D., Petersen B.L., Glawischnig E., Jensen A.B.,
Andreasson E., Halkier B.A.;
"Modulation of CYP79 genes and glucosinolate profiles in Arabidopsis
by defense signaling pathways.";
Plant Physiol. 131:298-308(2003).
[9]
FUNCTION.
STRAIN=cv. Wassilewskija;
PubMed=15194821; DOI=10.1104/pp.104.040113;
Tantikanjana T., Mikkelsen M.D., Hussain M., Halkier B.A.,
Sundaresan V.;
"Functional analysis of the tandem-duplicated P450 genes
SPS/BUS/CYP79F1 and CYP79F2 in glucosinolate biosynthesis and plant
development by Ds transposition-generated double mutants.";
Plant Physiol. 135:840-848(2004).
-!- FUNCTION: Catalyzes the conversion of the short chain elongated
methionines di-, tri-, and tetrahomomethionine to their respective
aldoximes 5-methylthiopentanaldoxime, 6-methylthiohexanaldoxime,
and 7-methylheptanaldoxime. {ECO:0000269|PubMed:11133994,
ECO:0000269|PubMed:11226190, ECO:0000269|PubMed:15194821}.
-!- CATALYTIC ACTIVITY: An L-polyhomomethionine + 2 O(2) + 2 [reduced
NADPH--hemoprotein reductase] = an omega-(methylthio)-(E)-alkanal
oxime + CO(2) + 3 H(2)O + 2 [oxidized NADPH--hemoprotein
reductase]. {ECO:0000269|PubMed:11133994,
ECO:0000269|PubMed:12609033}.
-!- CATALYTIC ACTIVITY: Dihomomethionine + 2 O(2) + 2 [reduced NADPH--
hemoprotein reductase] = 5-methylthiopentanaldoxime + 3 H(2)O +
CO(2) + 2 [oxidized NADPH--hemoprotein reductase].
{ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033}.
-!- CATALYTIC ACTIVITY: Trihomomethionine + 2 O(2) + 2 [reduced
NADPH--hemoprotein reductase] = 6-methylthiohexanaldoxime + 3
H(2)O + CO(2) + 2 [oxidized NADPH--hemoprotein reductase].
{ECO:0000269|PubMed:11133994, ECO:0000269|PubMed:12609033}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=34 uM for dihomomethionine {ECO:0000269|PubMed:12609033};
KM=37 uM for trihomomethionine {ECO:0000269|PubMed:12609033};
KM=194 uM for tetrahomomethionine {ECO:0000269|PubMed:12609033};
KM=216 uM for pentahomomethionine {ECO:0000269|PubMed:12609033};
KM=74 uM for hexahomomethionine {ECO:0000269|PubMed:12609033};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11226190}; Single-pass membrane protein
{ECO:0000269|PubMed:11226190}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q949U1-1; Sequence=Displayed;
Name=2;
IsoId=Q949U1-2; Sequence=VSP_030739, VSP_030740;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Highly expressed in cotyledons, leaves, stems
and siliques. Detected in flowers and lateral roots, but not in
the main root. Expressed only in the vascular bundles in apical
plant parts. {ECO:0000269|PubMed:11133994,
ECO:0000269|PubMed:11226190, ECO:0000269|PubMed:12609033}.
-!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:12529537}.
-!- DISRUPTION PHENOTYPE: Plants have a bushy phenotype with crinkled
leaves and retarded vascularization. {ECO:0000269|PubMed:11226190,
ECO:0000269|PubMed:12609033}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD34693.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AC006341; AAD34693.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE29447.1; -; Genomic_DNA.
EMBL; CP002684; AEE29448.1; -; Genomic_DNA.
EMBL; AY035021; AAK59526.1; -; mRNA.
EMBL; AY050890; AAK92827.1; -; mRNA.
EMBL; AY114074; AAM45122.1; -; mRNA.
EMBL; EF598753; ABR09166.1; -; Genomic_DNA.
EMBL; EF598754; ABR09167.1; -; Genomic_DNA.
EMBL; EF598755; ABR09168.1; -; Genomic_DNA.
EMBL; EF598756; ABR09169.1; -; Genomic_DNA.
EMBL; EF598757; ABR09170.1; -; Genomic_DNA.
EMBL; EF598758; ABR09171.1; -; Genomic_DNA.
EMBL; EF598759; ABR09172.1; -; Genomic_DNA.
EMBL; EF598760; ABR09173.1; -; Genomic_DNA.
EMBL; EF598761; ABR09174.1; -; Genomic_DNA.
EMBL; EF598762; ABR09175.1; -; Genomic_DNA.
EMBL; EF598763; ABR09176.1; -; Genomic_DNA.
EMBL; EF598764; ABR09177.1; -; Genomic_DNA.
EMBL; EF598765; ABR09178.1; -; Genomic_DNA.
EMBL; EF598766; ABR09179.1; -; Genomic_DNA.
EMBL; EF598767; ABR09180.1; -; Genomic_DNA.
EMBL; EF598768; ABR09181.1; -; Genomic_DNA.
EMBL; EF598769; ABR09182.1; -; Genomic_DNA.
EMBL; EF598770; ABR09183.1; -; Genomic_DNA.
EMBL; EF598771; ABR09184.1; -; Genomic_DNA.
EMBL; EF598772; ABR09185.1; -; Genomic_DNA.
EMBL; EF598773; ABR09186.1; -; Genomic_DNA.
EMBL; EF598774; ABR09187.1; -; Genomic_DNA.
EMBL; EF598775; ABR09188.1; -; Genomic_DNA.
EMBL; EF598776; ABR09189.1; -; Genomic_DNA.
PIR; D86299; D86299.
RefSeq; NP_563996.2; NM_101507.3. [Q949U1-1]
RefSeq; NP_973840.1; NM_202111.2. [Q949U1-2]
UniGene; At.11316; -.
ProteinModelPortal; Q949U1; -.
BioGrid; 23451; 3.
STRING; 3702.AT1G16410.1; -.
PaxDb; Q949U1; -.
PRIDE; Q949U1; -.
EnsemblPlants; AT1G16410.1; AT1G16410.1; AT1G16410. [Q949U1-1]
EnsemblPlants; AT1G16410.2; AT1G16410.2; AT1G16410. [Q949U1-2]
GeneID; 838211; -.
Gramene; AT1G16410.1; AT1G16410.1; AT1G16410.
Gramene; AT1G16410.2; AT1G16410.2; AT1G16410.
KEGG; ath:AT1G16410; -.
Araport; AT1G16410; -.
TAIR; locus:2032890; AT1G16410.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
InParanoid; Q949U1; -.
KO; K12154; -.
OMA; RAITINS; -.
OrthoDB; EOG093606WM; -.
PhylomeDB; Q949U1; -.
BioCyc; ARA:AT1G16410-MONOMER; -.
BioCyc; MetaCyc:AT1G16410-MONOMER; -.
PRO; PR:Q949U1; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q949U1; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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.
GO; GO:0098542; P:defense response to other organism; IBA:GO_Central.
GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
GO; GO:0009684; P:indoleacetic acid biosynthetic process; IBA:GO_Central.
GO; GO:0009625; P:response to insect; IEP:TAIR.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum; Heme;
Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 538 Dihomomethionine N-hydroxylase.
/FTId=PRO_0000315843.
TRANSMEM 8 28 Helical. {ECO:0000255}.
VAR_SEQ 417 423 SHIHVCR -> KKKKKKR (in isoform 2).
{ECO:0000305}.
/FTId=VSP_030739.
VAR_SEQ 424 538 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_030740.
VARIANT 43 43 C -> R (in strain: cv. Ag-0, cv. Br-0,
cv. C24, cv. Ct-1, cv. Edi-0, cv. Kas-1,
cv. Kin-0, cv. Landsberg erecta, cv. Ll-
0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-
1, cv. Nok-3, cv. Oy-0, cv. Sorbo, cv.
Van-0, cv. Wa-1 and cv. Wassilewskija).
VARIANT 83 83 A -> G (in strain: cv. Se-0).
VARIANT 120 120 I -> T (in strain: cv. Br-0 and cv. Mt-
0).
VARIANT 154 154 V -> F (in strain: cv. Ag-0, cv. Cvi-1,
cv. Edi-0, cv. Ll-0 and cv. Nok-3).
VARIANT 158 158 K -> N (in strain: cv. Ag-0, cv. Br-0,
cv. Cvi-1, cv. Edi-0, cv. Ll-0, cv. Lz-0,
cv. Mt-0, cv. Nok-3 and cv. Van-0).
VARIANT 159 159 M -> I (in strain: cv. Nd-1).
VARIANT 161 161 E -> K (in strain: cv. Lz-0 and cv. Van-
0).
VARIANT 192 192 R -> W (in strain: cv. Kin-0).
VARIANT 222 222 G -> V (in strain: cv. Ll-0).
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


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E1557b ELISA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
U1557b CLIA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T


 

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