C94B1_ARATH
ID C94B1_ARATH Reviewed; 510 AA.
AC Q9FMV7; Q8GWY4; Q8LGH8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome P450 94B1 {ECO:0000305};
DE EC=1.14.14.48 {ECO:0000269|PubMed:25210037};
DE AltName: Full=Jasmonoyl-L-amino acid 12-hydroxylase {ECO:0000303|PubMed:25210037};
GN Name=CYP94B1 {ECO:0000303|PubMed:21576464};
GN OrderedLocusNames=At5g63450 {ECO:0000312|Araport:AT5G63450};
GN ORFNames=MLE2.8 {ECO:0000312|EMBL:BAB08810.1};
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 [MRNA].
RA Civjan N.R., Duan H., Schuler M.A.;
RT "Arabidopsis CYP94B1 and CYP94C1: fatty acid hydroxylases induced by stress
RT signaling molecules.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
RP INDUCTION BY WOUNDING.
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
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. {ECO:0000269|PubMed:25210037}.
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:25210037};
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}.
CC -!- INDUCTION: Induced by wounding. {ECO:0000269|PubMed:21576464}.
CC -!- MISCELLANEOUS: Plants overexpressing CYP94B1 are jasmonate insensitive
CC and present developmental defects in all organs.
CC {ECO:0000269|PubMed:25210037}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM60854.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ201796; ABA61323.1; -; mRNA.
DR EMBL; AB007649; BAB08810.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97750.1; -; Genomic_DNA.
DR EMBL; AK118560; BAC43161.1; -; mRNA.
DR EMBL; BT005906; AAO64841.1; -; mRNA.
DR EMBL; AY084262; AAM60854.1; ALT_INIT; mRNA.
DR RefSeq; NP_201150.1; NM_125740.3.
DR AlphaFoldDB; Q9FMV7; -.
DR SMR; Q9FMV7; -.
DR BioGRID; 21706; 2.
DR IntAct; Q9FMV7; 1.
DR STRING; 3702.AT5G63450.1; -.
DR PaxDb; Q9FMV7; -.
DR PRIDE; Q9FMV7; -.
DR ProteomicsDB; 240273; -.
DR EnsemblPlants; AT5G63450.1; AT5G63450.1; AT5G63450.
DR GeneID; 836464; -.
DR Gramene; AT5G63450.1; AT5G63450.1; AT5G63450.
DR KEGG; ath:AT5G63450; -.
DR Araport; AT5G63450; -.
DR TAIR; locus:2167371; AT5G63450.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_2_1; -.
DR InParanoid; Q9FMV7; -.
DR OMA; WYTGLLA; -.
DR PhylomeDB; Q9FMV7; -.
DR BioCyc; ARA:GQT-1370-MON; -.
DR BioCyc; MetaCyc:GQT-1370-MON; -.
DR BRENDA; 1.14.14.48; 399.
DR PRO; PR:Q9FMV7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMV7; baseline and differential.
DR Genevisible; Q9FMV7; AT.
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:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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 Heme; Iron; Jasmonic acid signaling pathway; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..510
FT /note="Cytochrome P450 94B1"
FT /id="PRO_0000425852"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
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"
FT CONFLICT 1..2
FT /note="Missing (in Ref. 6; AAM60854)"
FT /evidence="ECO:0000305"
FT CONFLICT 39..42
FT /note="TSYQ -> ISYP (in Ref. 6; AAM60854)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="Y -> D (in Ref. 4; BAC43161 and 5; AAO64841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57782 MW; BBE376038AD517C4 CRC64;
MEMLNAIILI LFPIIGFVLI FSFPTKTLKA KTASPSNPTS YQLIGSILSF NKNRHRLLQW
YTDLLRLSPS QTITVDLLFG RRTIITANPE NVEHILKTNF YNFPKGKPFT DLLGDLLGGG
IFNSDGELWS SQRKLASHEF TMRSLREFTF EILREEVQNR LIPVLSSAVD CGETVDFQEV
LKRFAFDVVC KVSLGWDPDC LDLTRPVPEL VKAFDVAAEI SARRATEPVY AVWKVKRFLN
VGSEKRLREA IKTVHLSVSE IIRAKKKSLD IGGDVSDKQD LLSRFLAAGH GEEAVRDSVI
SFIMAGRDTT SAAMTWLFWL LSQNDDVETK ILDELRNKGS LGLGFEDLRE MSYTKACLCE
AMRLYPPVAW DSKHAANDDI LPDGTPLKKG DKVTYFPYGM GRMEKVWGKD WDEFKPNRWF
EEEPSYGTKP VLKSVSSFKF PVFQAGPRVC IGKEMAFTQM KYVVGSVLSR FKIIPVCNNR
PVFVPLLTAH MAGGLKVKIK RREQCDSMYI
