C81F3_ARATH
ID C81F3_ARATH Reviewed; 501 AA.
AC Q0WTF4; Q6NQ75; Q8LA85; Q9SZU0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytochrome P450 81F3 {ECO:0000305};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP81F3 {ECO:0000303|PubMed:21317374};
GN OrderedLocusNames=At4g37400 {ECO:0000312|Araport:AT4G37400};
GN ORFNames=F6G17.50 {ECO:0000312|EMBL:CAB38207.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-501.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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).
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 {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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035601; CAB38207.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161591; CAB80405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86788.1; -; Genomic_DNA.
DR EMBL; AK227603; BAE99594.1; -; mRNA.
DR EMBL; AY087977; AAM67337.1; -; mRNA.
DR EMBL; BT010585; AAQ89607.1; -; mRNA.
DR PIR; T04734; T04734.
DR RefSeq; NP_568025.1; NM_119903.4.
DR AlphaFoldDB; Q0WTF4; -.
DR SMR; Q0WTF4; -.
DR STRING; 3702.AT4G37400.1; -.
DR PaxDb; Q0WTF4; -.
DR PRIDE; Q0WTF4; -.
DR ProteomicsDB; 240532; -.
DR EnsemblPlants; AT4G37400.1; AT4G37400.1; AT4G37400.
DR GeneID; 829894; -.
DR Gramene; AT4G37400.1; AT4G37400.1; AT4G37400.
DR KEGG; ath:AT4G37400; -.
DR Araport; AT4G37400; -.
DR TAIR; locus:2126372; AT4G37400.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q0WTF4; -.
DR OMA; ELWNEPE; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q0WTF4; -.
DR BioCyc; ARA:AT4G37400-MON; -.
DR PRO; PR:Q0WTF4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WTF4; 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:0004497; F:monooxygenase activity; IDA:TAIR.
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:0042343; P:indole glucosinolate metabolic process; IDA: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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Cytochrome P450 81F3"
FT /id="PRO_0000435493"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 435
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"
FT CONFLICT 17
FT /note="Y -> N (in Ref. 4; AAM67337)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="N -> K (in Ref. 4; AAM67337)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="K -> R (in Ref. 4; AAM67337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 56637 MW; 9319BDD7F309FB69 CRC64;
MFYYVIVLPL ALFLLAYKLF FTSKTKRFNL PPSPPYSLPI LGHHNLLKPP VHRLFHRLSK
THGPIFSLQF GSRRAVVISS SSLATQCFTG QNDIILSNRP CFLTAKYVAY NYTTVGTAPY
GDHWRNLRRI CSLEILSSNR LTNFLHIRKD EIHRMLTRLS RDVNKEIELE PLLSDLTFNN
IVRMVTGKRY YGDEVHNEEE ANVFKKLVAD INDCSGARHP GDYLPFMKMF GGSFEKKVKA
LAEAMDEILQ RLLEECKRDK DGNTMVNHLL SLQQNEPEYY TDVTIKGLML GMMIAGTDTS
AVTLEWAMSS LLNHPEALEK AKLEIDEKIG QERLIDEPDI ANLPYLQNIV SETFRLYPAA
PLLVPRSPTE DIKVGGYDVP RGTMVMVNAW AIHRDPELWN EPEKFKPERF NGGEGGGRGE
DVHKLMPFGN GRRSCPGAGL GQKIVTLALG SLIQCFDWQK VNGEAIDMTE TPGMAMRKKI
PLSALCQSRP IMSKLQAHLK G
