C81F1_ARATH
ID C81F1_ARATH Reviewed; 500 AA.
AC O65790; Q7FBW2; Q8LBE7; Q9SZU3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytochrome P450 81F1 {ECO:0000305};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP81F1 {ECO:0000303|PubMed:21317374}; Synonyms=CYP91A2;
GN OrderedLocusNames=At4g37430; ORFNames=F6G17.80;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9620263; DOI=10.1023/a:1005921406884;
RA Mizutani M., Ward E., Ohta D.;
RT "Cytochrome P450 superfamily in Arabidopsis thaliana: isolation of cDNAs,
RT differential expression, and RFLP mapping of multiple cytochromes P450.";
RL Plant Mol. Biol. 37:39-52(1998).
RN [2]
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 [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 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 [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:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D78607; BAA28539.1; -; mRNA.
DR EMBL; AL035601; CAB38210.1; -; Genomic_DNA.
DR EMBL; AL161591; CAB80408.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86792.1; -; Genomic_DNA.
DR EMBL; AY039844; AAK63948.1; -; mRNA.
DR EMBL; AY087256; AAM67324.1; -; mRNA.
DR PIR; T04737; T04737.
DR PIR; T52175; T52175.
DR RefSeq; NP_195459.1; NM_119906.3.
DR AlphaFoldDB; O65790; -.
DR SMR; O65790; -.
DR STRING; 3702.AT4G37430.1; -.
DR iPTMnet; O65790; -.
DR PaxDb; O65790; -.
DR PRIDE; O65790; -.
DR ProteomicsDB; 239168; -.
DR EnsemblPlants; AT4G37430.1; AT4G37430.1; AT4G37430.
DR GeneID; 829897; -.
DR Gramene; AT4G37430.1; AT4G37430.1; AT4G37430.
DR KEGG; ath:AT4G37430; -.
DR Araport; AT4G37430; -.
DR TAIR; locus:2126402; AT4G37430.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; O65790; -.
DR OMA; YSGANHS; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; O65790; -.
DR BioCyc; ARA:AT4G37430-MON; -.
DR PRO; PR:O65790; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65790; differential.
DR Genevisible; O65790; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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; Isopeptide bond; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..500
FT /note="Cytochrome P450 81F1"
FT /id="PRO_0000052161"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 438
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 CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SZU1"
FT CONFLICT 102
FT /note="A -> S (in Ref. 5; AAM67324)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="A -> V (in Ref. 1; BAA28539)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="I -> M (in Ref. 1; BAA28539)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="N -> I (in Ref. 1; BAA28539)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="S -> T (in Ref. 1; BAA28539)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="M -> I (in Ref. 5; AAM67324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 57555 MW; 0FB453D2070EA2EA CRC64;
MLYFILLPLL FLVISYKFLY SKTQRFNLPP GPPSRPFVGH LHLMKPPIHR LLQRYSNQYG
PIFSLRFGSR RVVVITSPSL AQESFTGQND IVLSSRPLQL TAKYVAYNHT TVGTAPYGDH
WRNLRRICSQ EILSSHRLIN FQHIRKDEIL RMLTRLSRYT QTSNESNDFT HIELEPLLSD
LTFNNIVRMV TGKRYYGDDV NNKEEAELFK KLVYDIAMYS GANHSADYLP ILKLFGNKFE
KEVKAIGKSM DDILQRLLDE CRRDKEGNTM VNHLISLQQQ QPEYYTDVII KGLMMSMMLA
GTETSAVTLE WAMANLLRNP EVLEKARSEI DEKIGKDRLI DESDIAVLPY LQNVVSETFR
LFPVAPFLIP RSPTDDMKIG GYDVPRDTIV MVNAWAIHRD PEIWEEPEKF NPDRYNDGCG
SDYYVYKLMP FGNGRRTCPG AGLGQRIVTL ALGSLIQCFE WENVKGEEMD MSESTGLGMR
KMDPLRAMCR PRPIMSKLLL
