C81F2_ARATH
ID C81F2_ARATH Reviewed; 491 AA.
AC Q9LVD6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome P450 81F2 {ECO:0000305};
DE EC=1.14.-.- {ECO:0000305};
DE AltName: Full=Protein INDOLE GLUCOSINOLATE MODIFIER 1 {ECO:0000303|PubMed:19293369};
GN Name=CYP81F2 {ECO:0000303|PubMed:21317374};
GN Synonyms=IGM1 {ECO:0000303|PubMed:19293369};
GN OrderedLocusNames=At5g57220 {ECO:0000312|Araport:AT5G57220};
GN ORFNames=MJB24.3 {ECO:0000312|EMBL:BAA96945.1};
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 [GENOMIC DNA].
RX PubMed=19293369; DOI=10.1105/tpc.108.063115;
RA Pfalz M., Vogel H., Kroymann J.;
RT "The gene controlling the indole glucosinolate modifier1 quantitative trait
RT locus alters indole glucosinolate structures and aphid resistance in
RT Arabidopsis.";
RL Plant Cell 21:985-999(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=19095900; DOI=10.1126/science.1163732;
RA Bednarek P., Pislewska-Bednarek M., Svatos A., Schneider B., Doubsky J.,
RA Mansurova M., Humphry M., Consonni C., Panstruga R., Sanchez-Vallet A.,
RA Molina A., Schulze-Lefert P.;
RT "A glucosinolate metabolism pathway in living plant cells mediates broad-
RT spectrum antifungal defense.";
RL Science 323:101-106(2009).
RN [6]
RP FUNCTION.
RX PubMed=20605856; DOI=10.1105/tpc.110.074344;
RA Hiruma K., Onozawa-Komori M., Takahashi F., Asakura M., Bednarek P.,
RA Okuno T., Schulze-Lefert P., Takano Y.;
RT "Entry mode-dependent function of an indole glucosinolate pathway in
RT Arabidopsis for nonhost resistance against anthracnose pathogens.";
RL Plant Cell 22:2429-2443(2010).
RN [7]
RP FUNCTION.
RX PubMed=20408997; DOI=10.1111/j.1365-313x.2010.04224.x;
RA Sanchez-Vallet A., Ramos B., Bednarek P., Lopez G., Pislewska-Bednarek M.,
RA Schulze-Lefert P., Molina A.;
RT "Tryptophan-derived secondary metabolites in Arabidopsis thaliana confer
RT non-host resistance to necrotrophic Plectosphaerella cucumerina fungi.";
RL Plant J. 63:115-127(2010).
RN [8]
RP FUNCTION.
RX PubMed=21317374; DOI=10.1105/tpc.110.081711;
RA Pfalz M., Mikkelsen M.D., Bednarek P., Olsen C.E., Halkier B.A.,
RA Kroymann J.;
RT "Metabolic engineering in Nicotiana benthamiana reveals key enzyme
RT functions in Arabidopsis indole glucosinolate modification.";
RL Plant Cell 23:716-729(2011).
RN [9]
RP INDUCTION.
RX PubMed=22947164; DOI=10.1111/j.1364-3703.2012.00827.x;
RA Po-Wen C., Singh P., Zimmerli L.;
RT "Priming of the Arabidopsis pattern-triggered immunity response upon
RT infection by necrotrophic Pectobacterium carotovorum bacteria.";
RL Mol. Plant Pathol. 14:58-70(2013).
CC -!- FUNCTION: Involved in indole glucosinolate biosynthesis. Catalyzes
CC hydroxylation reactions of the glucosinolate indole ring. Converts
CC indol-3-yl-methylglucosinolate (I3M) to 4-hydroxy-indol-3-yl-
CC methylglucosinolate (4OH-I3M) and/or 1-hydroxy-indol-3-yl-
CC methylglucosinolate (1OH-I3M) intermediates. These hydroxy
CC intermediates are converted to 4-methoxy-indol-3-yl-methylglucosinolate
CC (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate (1MO-I3M) by
CC indole glucosinolate methyltransferase 1 and 2 (IGMT1 and IGMT2)
CC (PubMed:21317374). Contributes to defense against the green peach aphid
CC (Myzus persicae), a generalist phloem-feeding herbivore
CC (PubMed:19293369). Required for the biosynthesis of antifungal indole
CC glucosinolate metabolites (PubMed:19095900, PubMed:20605856,
CC PubMed:20408997, PubMed:21317374). Required for the pathogen-induced
CC accumulation of 4MO-I3M, which in turn is activated by the atypical
CC BGLU26/PEN2 myrosinase (PubMed:19095900). Required for the biosynthesis
CC of Trp-derived antifungal compounds and non-host resistance to the
CC necrotrophic fungal pathogen Plectosphaerella cucumerina
CC (PubMed:20408997). Required for resistance to the non-adapted fungal
CC pathogen Colletotrichum gloeosporioides (PubMed:20605856).
CC {ECO:0000269|PubMed:19095900, ECO:0000269|PubMed:19293369,
CC ECO:0000269|PubMed:20408997, ECO:0000269|PubMed:20605856,
CC ECO:0000269|PubMed:21317374}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: By beta-aminobutyric acid (BABA) and elicitors of pattern-
CC triggered immunity (PTI), such as flg22 and elf26 peptides.
CC {ECO:0000269|PubMed:22947164}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; FM208179; CAR63887.1; -; Genomic_DNA.
DR EMBL; AB019233; BAA96945.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96867.1; -; Genomic_DNA.
DR EMBL; AY065209; AAL38685.1; -; mRNA.
DR EMBL; AY096511; AAM20161.1; -; mRNA.
DR RefSeq; NP_200532.1; NM_125104.3.
DR AlphaFoldDB; Q9LVD6; -.
DR SMR; Q9LVD6; -.
DR STRING; 3702.AT5G57220.1; -.
DR PaxDb; Q9LVD6; -.
DR PRIDE; Q9LVD6; -.
DR ProteomicsDB; 240531; -.
DR EnsemblPlants; AT5G57220.1; AT5G57220.1; AT5G57220.
DR GeneID; 835828; -.
DR Gramene; AT5G57220.1; AT5G57220.1; AT5G57220.
DR KEGG; ath:AT5G57220; -.
DR Araport; AT5G57220; -.
DR TAIR; locus:2165635; AT5G57220.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9LVD6; -.
DR OMA; EMINEMM; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9LVD6; -.
DR BioCyc; ARA:AT5G57220-MON; -.
DR BioCyc; MetaCyc:AT5G57220-MON; -.
DR PRO; PR:Q9LVD6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVD6; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0002213; P:defense response to insect; IMP:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0009759; P:indole glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0042343; P:indole glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; 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 PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Cytochrome P450 81F2"
FT /id="PRO_0000435492"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 429
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|UniProtKB:Q96242"
SQ 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
