YUC8_ORYSI
ID YUC8_ORYSI Reviewed; 421 AA.
AC B8ANW0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Indole-3-pyruvate monooxygenase YUCCA8 {ECO:0000305};
DE Short=OsYUCCA8 {ECO:0000305};
DE EC=1.14.13.168 {ECO:0000250|UniProtKB:Q10RE2};
DE AltName: Full=Flavin-containing monooxygenase YUCCA8 {ECO:0000305};
DE AltName: Full=OsFMOt {ECO:0000303|PubMed:24371168};
DE AltName: Full=Protein CONSTITUTIVELY WILTED 1 {ECO:0000305};
DE Short=OsCOW1 {ECO:0000305};
DE AltName: Full=Protein NARROW LEAF 7 {ECO:0000305};
DE AltName: Full=Protein RICE ETHYLENE-INSENSITIVE 7 {ECO:0000305};
GN Name=YUCCA8 {ECO:0000305};
GN Synonyms=COW1 {ECO:0000305}, NAL7 {ECO:0000305}, REIN7 {ECO:0000305},
GN YUCA8 {ECO:0000305}; ORFNames=OsI_10125 {ECO:0000312|EMBL:EEC74567.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Qinghuazhan;
RX PubMed=24371168; DOI=10.1007/s12041-013-0297-0;
RA Yi J., Liu L., Cao Y., Li J., Mei M.;
RT "Cloning, characterization and expression of OsFMO(t) in rice encoding a
RT flavin monooxygenase.";
RL J. Genet. 92:471-480(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Qinghuazhan;
RX DOI=10.1111/j.1744-7909.2007.00572.x;
RA Yi J., Zhuang C., Wang X., Cao Y., Liu Y., Li J., Mei M.;
RT "Genetic analysis and molecular mapping of a rolling leaf mutation gene in
RT rice.";
RL J. Integr. Plant Biol. 49:1746-1753(2007).
CC -!- FUNCTION: Involved in auxin biosynthesis (PubMed:24371168). Converts
CC the indole-3-pyruvic acid (IPA) produced by the TAA family to indole-3-
CC acetic acid (IAA) (By similarity). Seems not able to use tryptamine
CC (TAM) as substrate (By similarity). Probably responsible for auxin
CC biosynthesis in leaves and involved in the regulation of lateral leaf
CC growth (Ref.3). Required for maintaining water homeostasis and an
CC appropriate root to shoot ratio (By similarity). Required for the
CC inhibition of root growth by ethylene in etiolated seedlings (By
CC similarity). Functions downstream of the ethylene-response
CC transcription factor EIL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q10RE2, ECO:0000269|PubMed:24371168,
CC ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.168;
CC Evidence={ECO:0000250|UniProtKB:Q10RE2};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q10RE2};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q10RE2}.
CC -!- TISSUE SPECIFICITY: Expressed in organs undergoing active growth and
CC cell division. {ECO:0000269|PubMed:24371168}.
CC -!- DISRUPTION PHENOTYPE: Narrow and rolled leaf phenotype.
CC {ECO:0000269|Ref.3}.
CC -!- MISCELLANEOUS: Calli overexpressing YUCCA8 contain increased levels of
CC auxin and exhibit overgrowing roots and abnormal root morphology.
CC {ECO:0000269|PubMed:24371168}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; HQ443270; AED99265.1; -; Genomic_DNA.
DR EMBL; HQ443271; AED99266.1; -; mRNA.
DR EMBL; CM000128; EEC74567.1; -; Genomic_DNA.
DR AlphaFoldDB; B8ANW0; -.
DR SMR; B8ANW0; -.
DR STRING; 39946.B8ANW0; -.
DR EnsemblPlants; BGIOSGA011917-TA; BGIOSGA011917-PA; BGIOSGA011917.
DR Gramene; BGIOSGA011917-TA; BGIOSGA011917-PA; BGIOSGA011917.
DR HOGENOM; CLU_006909_2_0_1; -.
DR OMA; CELPHAR; -.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:2000024; P:regulation of leaf development; IEA:EnsemblPlants.
DR GO; GO:2000280; P:regulation of root development; IEA:EnsemblPlants.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..421
FT /note="Indole-3-pyruvate monooxygenase YUCCA8"
FT /id="PRO_0000445281"
FT BINDING 30..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 201..206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 45720 MW; 02974A5ACF7DAE3D CRC64;
MQGQQKQNAG GGGGDNASPC IVLDGPIIVG AGPSGLAVAA TLRQHGAPFT VVERSGGVAD
LWTNRTYDRL RLHLPKVFCE LPHVAFPPDF PTYPTKHDFL RYLHSYAARF AIAPLLRRTV
TRAWYDHPAS LWRVTTTTTS SSATSVITEY ASPWLVVASG ENAEVVVPKV KGRERFAGEA
LHSSEYRSGE RFRGMRVLVV GCGNSGMEMC LDLCEHGAMP FMSVRSGVHV LPREMFGAST
FGIAMKLLRW LPIKMVDRFL LLVARMVLGD TEKYGLKRPK LGPLEIKNIT GKSPVLDVGA
WSLIKSGNIK IVPEVESFSG NGARFVDGNE MAFDAVIFAT GYRSNVPSWL QEDGELFTEE
GKLRSSGSSS EWRWRGPNGL YCVGFSGRGL LGAGADALRA AADIAGRWQE TQQAAANISS
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