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Cytochrome P450 81F2 (EC 1.14.-.-) (Protein INDOLE GLUCOSINOLATE MODIFIER 1)

 C81F2_ARATH             Reviewed;         491 AA.
Q9LVD6;
17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
07-NOV-2018, entry version 135.
RecName: Full=Cytochrome P450 81F2 {ECO:0000305};
EC=1.14.-.- {ECO:0000305};
AltName: Full=Protein INDOLE GLUCOSINOLATE MODIFIER 1 {ECO:0000303|PubMed:19293369};
Name=CYP81F2 {ECO:0000303|PubMed:21317374};
Synonyms=IGM1 {ECO:0000303|PubMed:19293369};
OrderedLocusNames=At5g57220 {ECO:0000312|Araport:AT5G57220};
ORFNames=MJB24.3 {ECO:0000312|EMBL:BAA96945.1};
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 [GENOMIC DNA].
PubMed=19293369; DOI=10.1105/tpc.108.063115;
Pfalz M., Vogel H., Kroymann J.;
"The gene controlling the indole glucosinolate modifier1 quantitative
trait locus alters indole glucosinolate structures and aphid
resistance in Arabidopsis.";
Plant Cell 21:985-999(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
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).
[5]
FUNCTION.
PubMed=19095900; DOI=10.1126/science.1163732;
Bednarek P., Pislewska-Bednarek M., Svatos A., Schneider B.,
Doubsky J., Mansurova M., Humphry M., Consonni C., Panstruga R.,
Sanchez-Vallet A., Molina A., Schulze-Lefert P.;
"A glucosinolate metabolism pathway in living plant cells mediates
broad-spectrum antifungal defense.";
Science 323:101-106(2009).
[6]
FUNCTION.
PubMed=20605856; DOI=10.1105/tpc.110.074344;
Hiruma K., Onozawa-Komori M., Takahashi F., Asakura M., Bednarek P.,
Okuno T., Schulze-Lefert P., Takano Y.;
"Entry mode-dependent function of an indole glucosinolate pathway in
Arabidopsis for nonhost resistance against anthracnose pathogens.";
Plant Cell 22:2429-2443(2010).
[7]
FUNCTION.
PubMed=20408997; DOI=10.1111/j.1365-313X.2010.04224.x;
Sanchez-Vallet A., Ramos B., Bednarek P., Lopez G.,
Pislewska-Bednarek M., Schulze-Lefert P., Molina A.;
"Tryptophan-derived secondary metabolites in Arabidopsis thaliana
confer non-host resistance to necrotrophic Plectosphaerella cucumerina
fungi.";
Plant J. 63:115-127(2010).
[8]
FUNCTION.
PubMed=21317374; DOI=10.1105/tpc.110.081711;
Pfalz M., Mikkelsen M.D., Bednarek P., Olsen C.E., Halkier B.A.,
Kroymann J.;
"Metabolic engineering in Nicotiana benthamiana reveals key enzyme
functions in Arabidopsis indole glucosinolate modification.";
Plant Cell 23:716-729(2011).
[9]
INDUCTION.
PubMed=22947164; DOI=10.1111/j.1364-3703.2012.00827.x;
Po-Wen C., Singh P., Zimmerli L.;
"Priming of the Arabidopsis pattern-triggered immunity response upon
infection by necrotrophic Pectobacterium carotovorum bacteria.";
Mol. Plant Pathol. 14:58-70(2013).
-!- FUNCTION: Involved in indole glucosinolate biosynthesis. Catalyzes
hydroxylation reactions of the glucosinolate indole ring. Converts
indol-3-yl-methylglucosinolate (I3M) to 4-hydroxy-indol-3-yl-
methylglucosinolate (4OH-I3M) and/or 1-hydroxy-indol-3-yl-
methylglucosinolate (1OH-I3M) intermediates. These hydroxy
intermediates are converted to 4-methoxy-indol-3-yl-
methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-
methylglucosinolate (1MO-I3M) by indole glucosinolate
methyltransferase 1 and 2 (IGMT1 and IGMT2) (PubMed:21317374).
Contributes to defense against the green peach aphid (Myzus
persicae), a generalist phloem-feeding herbivore
(PubMed:19293369). Required for the biosynthesis of antifungal
indole glucosinolate metabolites (PubMed:19095900,
PubMed:20605856, PubMed:20408997, PubMed:21317374). Required for
the pathogen-induced accumulation of 4MO-I3M, which in turn is
activated by the atypical BGLU26/PEN2 myrosinase
(PubMed:19095900). Required for the biosynthesis of Trp-derived
antifungal compounds and non-host resistance to the necrotrophic
fungal pathogen Plectosphaerella cucumerina (PubMed:20408997).
Required for resistance to the non-adapted fungal pathogen
Colletotrichum gloeosporioides (PubMed:20605856).
{ECO:0000269|PubMed:19095900, ECO:0000269|PubMed:19293369,
ECO:0000269|PubMed:20408997, ECO:0000269|PubMed:20605856,
ECO:0000269|PubMed:21317374}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:Q96242};
-!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
protein {ECO:0000255}.
-!- INDUCTION: By beta-aminobutyric acid (BABA) and elicitors of
pattern-triggered immunity (PTI), such as flg22 and elf26
peptides. {ECO:0000269|PubMed:22947164}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; FM208179; CAR63887.1; -; Genomic_DNA.
EMBL; AB019233; BAA96945.1; -; Genomic_DNA.
EMBL; CP002688; AED96867.1; -; Genomic_DNA.
EMBL; AY065209; AAL38685.1; -; mRNA.
EMBL; AY096511; AAM20161.1; -; mRNA.
RefSeq; NP_200532.1; NM_125104.3.
UniGene; At.28563; -.
ProteinModelPortal; Q9LVD6; -.
SMR; Q9LVD6; -.
STRING; 3702.AT5G57220.1; -.
PaxDb; Q9LVD6; -.
EnsemblPlants; AT5G57220.1; AT5G57220.1; AT5G57220.
GeneID; 835828; -.
Gramene; AT5G57220.1; AT5G57220.1; AT5G57220.
KEGG; ath:AT5G57220; -.
Araport; AT5G57220; -.
TAIR; locus:2165635; AT5G57220.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
InParanoid; Q9LVD6; -.
KO; K00517; -.
OMA; DCTITSG; -.
OrthoDB; EOG09360EOO; -.
PhylomeDB; Q9LVD6; -.
BioCyc; ARA:AT5G57220-MONOMER; -.
BioCyc; MetaCyc:AT5G57220-MONOMER; -.
PRO; PR:Q9LVD6; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LVD6; baseline and differential.
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; IBA:GO_Central.
GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0002213; P:defense response to insect; IMP:TAIR.
GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
GO; GO:0009759; P:indole glucosinolate biosynthetic process; IMP:TAIR.
GO; GO:0042343; P:indole glucosinolate metabolic process; IMP:TAIR.
GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
GO; GO:0009617; P:response to bacterium; IMP: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.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
2: Evidence at transcript level;
Complete proteome; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
Oxidoreductase; Plant defense; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 491 Cytochrome P450 81F2.
/FTId=PRO_0000435492.
TRANSMEM 283 303 Helical. {ECO:0000255}.
METAL 429 429 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:Q96242}.
SEQUENCE 491 AA; 55693 MW; D38C16D3E8B66804 CRC64;
MDYVLIVLPL ALFLIAYKFL FSSKTQGFNL PPGPTPFPIV GHLHLVKPPV HRLFRRFAEK
YGDIFSLRYG SRQVVVISSL PLVRESFTGQ NDVILTNRPH FLTAKYVAYD YTTIGTAAYG
DHWRNLRRIC SLEILSSNRL TGFLSVRKDE IRRLLTKLSR EYDGRVVELE PLLADLTFNN
IVRMVTGRRY YGDQVHNKEE ANLFKKLVTD INDNSGASHP GDYLPILKVF GHGYEKKVKA
LGEAMDAFLQ RLLDECRING ESNTMVSHLL SLQLDQPKYY SDVIIKGLML SMMLAGTDTA
AVTLEWAMAN LLKKPEVLKK AKAEIDEKIG EERLVDEPDI ANLPYLQNIV SETFRLCPAA
PLLVPRSPSE DLKIGGYDIP RGTIVLVNAW AIHRDPRLWD EPEKFMPERF EDQEASKKLM
VFGNGRRTCP GATLGQRMVL LALGSLIQCF DWEKVNGEDV DMTENPGMAM RKLVQLRAVC
HKRPIMTNLL A


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