C94B3_ARATH
ID C94B3_ARATH Reviewed; 506 AA.
AC Q9SMP5;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytochrome P450 94B3 {ECO:0000305};
DE EC=1.14.14.48 {ECO:0000269|PubMed:21576464, ECO:0000269|PubMed:22215670};
DE AltName: Full=Jasmonoyl-L-amino acid 12-hydroxylase {ECO:0000303|PubMed:24467969};
DE AltName: Full=Jasmonoyl-isoleucine-12-hydroxylase {ECO:0000303|PubMed:21849397};
GN Name=CYP94B3 {ECO:0000303|PubMed:21576464};
GN OrderedLocusNames=At3g48520 {ECO:0000312|Araport:AT3G48520};
GN ORFNames=T8P19.30 {ECO:0000312|EMBL:CAB62341.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, INDUCTION BY WOUNDING, AND DISRUPTION PHENOTYPE.
RX PubMed=21849397; DOI=10.1093/pcp/pcr110;
RA Kitaoka N., Matsubara T., Sato M., Takahashi K., Wakuta S., Kawaide H.,
RA Matsui H., Nabeta K., Matsuura H.;
RT "Arabidopsis CYP94B3 encodes jasmonyl-L-isoleucine 12-hydroxylase, a key
RT enzyme in the oxidative catabolism of jasmonate.";
RL Plant Cell Physiol. 52:1757-1765(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY WOUNDING, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21576464; DOI=10.1073/pnas.1103542108;
RA Koo A.J., Cooke T.F., Howe G.A.;
RT "Cytochrome P450 CYP94B3 mediates catabolism and inactivation of the plant
RT hormone jasmonoyl-L-isoleucine.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9298-9303(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY WOUNDING, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22215670; DOI=10.1074/jbc.m111.316364;
RA Heitz T., Widemann E., Lugan R., Miesch L., Ullmann P., Desaubry L.,
RA Holder E., Grausem B., Kandel S., Miesch M., Werck-Reichhart D., Pinot F.;
RT "Cytochromes P450 CYP94C1 and CYP94B3 catalyze two successive oxidation
RT steps of plant hormone jasmonoyl-isoleucine for catabolic turnover.";
RL J. Biol. Chem. 287:6296-6306(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=25210037; DOI=10.1074/jbc.m114.603084;
RA Koo A.J., Thireault C., Zemelis S., Poudel A.N., Zhang T., Kitaoka N.,
RA Brandizzi F., Matsuura H., Howe G.A.;
RT "Endoplasmic reticulum-associated inactivation of the hormone jasmonoyl-L-
RT isoleucine by multiple members of the cytochrome P450 94 family in
RT Arabidopsis.";
RL J. Biol. Chem. 289:29728-29738(2014).
RN [9]
RP FUNCTION.
RX PubMed=24467969; DOI=10.1016/j.phytochem.2013.12.019;
RA Kitaoka N., Kawaide H., Amano N., Matsubara T., Nabeta K., Takahashi K.,
RA Matsuura H.;
RT "CYP94B3 activity against jasmonic acid amino acid conjugates and the
RT elucidation of 12-O-beta-glucopyranosyl-jasmonoyl-L-isoleucine as an
RT additional metabolite.";
RL Phytochemistry 99:6-13(2014).
CC -!- FUNCTION: Hydroxylase involved in the oxidation of the plant hormone
CC jasmonoyl-L-isoleucine (JA-Ile), a bioactive phytohormone of the
CC jasmonate-mediated signaling pathway. Converts JA-Ile to 12-hydroxy-JA-
CC Ile (PubMed:21576464, PubMed:21849397, PubMed:22215670). Exerts
CC negative feedback control on JA-Ile levels and plays a key role in
CC attenuation of jasmonate responses. Negatively regulates the expression
CC of wound-induced genes TIFY11A/JAZ5, TIFY5A/JAZ8 and TIFY5A/JAZ10
CC (PubMed:21576464). Catalyzes the hydroxylation of jasmonoyl-L-valine
CC (JA-Val), jasmonoyl-L-leucine (JA-Leu) and jasmonoyl-L-phenylalanine
CC (JA-Phe) in vitro. Converts JA-Val, JA-Leu and JA-Phe to 12-hydroxy-JA-
CC Val, 12-hydroxy-JA-Leu and 12-hydroxy-JA-Phe, respectively
CC (PubMed:24467969). {ECO:0000269|PubMed:21576464,
CC ECO:0000269|PubMed:21849397, ECO:0000269|PubMed:22215670,
CC ECO:0000269|PubMed:24467969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a jasmonyl-L-amino acid + O2 + reduced [NADPH--hemoprotein
CC reductase] = a 12-hydroxyjasmonyl-L-alpha-amino acid + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54832,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:136183, ChEBI:CHEBI:138374;
CC EC=1.14.14.48; Evidence={ECO:0000269|PubMed:21576464,
CC ECO:0000269|PubMed:22215670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54833;
CC Evidence={ECO:0000269|PubMed:21576464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-isoleucine-(+)-7-isojasmonate + NADPH + O2 = H2O + L-
CC isoleucine-(+)-12-hydroxy-7-isojasmonate + NADP(+);
CC Xref=Rhea:RHEA:54808, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:136180, ChEBI:CHEBI:136181;
CC Evidence={ECO:0000269|PubMed:21576464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54809;
CC Evidence={ECO:0000269|PubMed:21576464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a jasmonyl-L-isoleucinate + H(+) + NADPH + O2 = H2O + L-
CC isoleucine-12-hydroxyjasmonate + NADP(+); Xref=Rhea:RHEA:55164,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138626,
CC ChEBI:CHEBI:138627; Evidence={ECO:0000269|PubMed:21576464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55165;
CC Evidence={ECO:0000269|PubMed:21576464};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25210037}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:21576464,
CC ECO:0000269|PubMed:21849397, ECO:0000269|PubMed:22215670}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants accumulate high amounts of JA-Ile and
CC have strongly reduced levels of 12-hydroxy-JA-Ile in response to
CC wounding. {ECO:0000269|PubMed:21576464, ECO:0000269|PubMed:21849397,
CC ECO:0000269|PubMed:22215670}.
CC -!- MISCELLANEOUS: Plants over-expressing CAP94B3 are deficient in
CC jasmonate perception. {ECO:0000305|PubMed:21576464}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AL133315; CAB62341.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78426.1; -; Genomic_DNA.
DR EMBL; BT015332; AAU05455.1; -; mRNA.
DR EMBL; BT015841; AAU94404.1; -; mRNA.
DR EMBL; AK226339; BAE98488.1; -; mRNA.
DR PIR; T46196; T46196.
DR RefSeq; NP_190421.1; NM_114710.3.
DR AlphaFoldDB; Q9SMP5; -.
DR SMR; Q9SMP5; -.
DR BioGRID; 9330; 3.
DR STRING; 3702.AT3G48520.1; -.
DR SwissLipids; SLP:000001770; -.
DR PaxDb; Q9SMP5; -.
DR PRIDE; Q9SMP5; -.
DR ProteomicsDB; 240274; -.
DR EnsemblPlants; AT3G48520.1; AT3G48520.1; AT3G48520.
DR GeneID; 824011; -.
DR Gramene; AT3G48520.1; AT3G48520.1; AT3G48520.
DR KEGG; ath:AT3G48520; -.
DR Araport; AT3G48520; -.
DR TAIR; locus:2114460; AT3G48520.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9SMP5; -.
DR OMA; ERGFMTA; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9SMP5; -.
DR BioCyc; ARA:AT3G48520-MON; -.
DR BioCyc; MetaCyc:AT3G48520-MON; -.
DR BRENDA; 1.14.14.48; 399.
DR PRO; PR:Q9SMP5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMP5; baseline and differential.
DR Genevisible; Q9SMP5; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0052694; F:jasmonoyl-isoleucine-12-hydroxylase activity; IDA:TAIR.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0048653; P:anther development; IMP:TAIR.
DR GO; GO:0002213; P:defense response to insect; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0048480; P:stigma development; IMP:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
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.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Jasmonic acid signaling pathway;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Cytochrome P450 94B3"
FT /id="PRO_0000425853"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 447
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"
SQ SEQUENCE 506 AA; 56933 MW; DF06C087D438A601 CRC64;
MAFLLSFLIL AFLITIIFFL SSSSTKKVQE NTTYGPPSYP LIGSILSFNK NRHRLLQWYT
ELLRLSPSQT ILVPLLGNRR TIITTNPLNV EYILKTNFFN FPKGKPFTDL LGDLLGGGIF
NVDGHSWSSQ RKLASHEFST RSLRSFAFEV LKDEVENRLV PVLSTAADVG TTVDLQDVLK
RFAFDVVCKV SLGWDPDCLD LTRPVNPLVE AFDTAAEISA RRATEPIYAV WKTKRVLNVG
SERKLREAIR TVHVLVSEIV RAKKKSLEIG TGAEAKQDLL SRFLAAGHNG EAVRDMVISF
IMAGRDTTSA AMTWLFWLLT ENDDVERKIL EEVDPLVSLG LGFEDLKEMA YTKACLCEAM
RLYPPVSWDS KHAANDDVLP DGTRVKRGDK VTYFPYGMGR METLWGTDSE EFNPNRWFDS
EPGSTRPVLK PISPYKFPVF QAGPRVCVGK EMAFMQMKYV VGSVLSRFEI VPVNKDRPVF
VPLLTAHMAG GLKVKIKRRS HILNNV
