YUC6_ARATH
ID YUC6_ARATH Reviewed; 417 AA.
AC Q8VZ59;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Indole-3-pyruvate monooxygenase YUCCA6;
DE EC=1.14.13.168;
DE AltName: Full=Flavin-containing monooxygenase YUCCA6;
DE AltName: Full=Protein HYPERTALL1;
GN Name=YUC6; Synonyms=HYT1, YUCCA6; OrderedLocusNames=At5g25620;
GN ORFNames=T14C9.160;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
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 [4]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=16818609; DOI=10.1101/gad.1415106;
RA Cheng Y., Dai X., Zhao Y.;
RT "Auxin biosynthesis by the YUCCA flavin monooxygenases controls the
RT formation of floral organs and vascular tissues in Arabidopsis.";
RL Genes Dev. 20:1790-1799(2006).
RN [5]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17461789; DOI=10.1111/j.1365-313x.2007.03101.x;
RA Hansen B.G., Kliebenstein D.J., Halkier B.A.;
RT "Identification of a flavin-monooxygenase as the S-oxygenating enzyme in
RT aliphatic glucosinolate biosynthesis in Arabidopsis.";
RL Plant J. 50:902-910(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17885085; DOI=10.1104/pp.107.104935;
RA Kim J.I., Sharkhuu A., Jin J.B., Li P., Jeong J.C., Baek D., Lee S.Y.,
RA Blakeslee J.J., Murphy A.S., Bohnert H.J., Hasegawa P.M., Yun D.J.,
RA Bressan R.A.;
RT "yucca6, a dominant mutation in Arabidopsis, affects auxin accumulation and
RT auxin-related phenotypes.";
RL Plant Physiol. 145:722-735(2007).
RN [7]
RP INDUCTION BY SPL.
RX PubMed=18557819; DOI=10.1111/j.1469-8137.2008.02514.x;
RA Li L.C., Qin G.J., Tsuge T., Hou X.H., Ding M.Y., Aoyama T., Oka A.,
RA Chen Z., Gu H., Zhao Y., Qu L.J.;
RT "SPOROCYTELESS modulates YUCCA expression to regulate the development of
RT lateral organs in Arabidopsis.";
RL New Phytol. 179:751-764(2008).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=18628351; DOI=10.1105/tpc.107.057570;
RA Cecchetti V., Altamura M.M., Falasca G., Costantino P., Cardarelli M.;
RT "Auxin regulates Arabidopsis anther dehiscence, pollen maturation, and
RT filament elongation.";
RL Plant Cell 20:1760-1774(2008).
RN [9]
RP INDUCTION BY HEAT.
RX PubMed=20421476; DOI=10.1073/pnas.1000869107;
RA Sakata T., Oshino T., Miura S., Tomabechi M., Tsunaga Y., Higashitani N.,
RA Miyazawa Y., Takahashi H., Watanabe M., Higashitani A.;
RT "Auxins reverse plant male sterility caused by high temperatures.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8569-8574(2010).
RN [10]
RP FUNCTION.
RX PubMed=22025721; DOI=10.1073/pnas.1108436108;
RA Won C., Shen X., Mashiguchi K., Zheng Z., Dai X., Cheng Y., Kasahara H.,
RA Kamiya Y., Chory J., Zhao Y.;
RT "Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN
RT AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18518-18523(2011).
RN [11]
RP FUNCTION.
RX PubMed=22986790; DOI=10.1093/mp/sss100;
RA Kim J.I., Baek D., Park H.C., Chun H.J., Oh D.H., Lee M.K., Cha J.Y.,
RA Kim W.Y., Kim M.C., Chung W.S., Bohnert H.J., Lee S.Y., Bressan R.A.,
RA Lee S.W., Yun D.J.;
RT "Overexpression of Arabidopsis YUCCA6 in potato results in high-auxin
RT developmental phenotypes and enhanced resistance to water deficit.";
RL Mol. Plant 6:337-349(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23188833; DOI=10.1074/jbc.m112.424077;
RA Dai X., Mashiguchi K., Chen Q., Kasahara H., Kamiya Y., Ojha S., Dubois J.,
RA Ballou D., Zhao Y.;
RT "The biochemical mechanism of auxin biosynthesis by an Arabidopsis YUCCA
RT flavin-containing monooxygenase.";
RL J. Biol. Chem. 288:1448-1457(2013).
CC -!- FUNCTION: Involved in auxin biosynthesis via the indole-3-pyruvic acid
CC (IPA) pathway. Also able to convert in vitro phenyl pyruvate (PPA) to
CC phenyl acetic acid (PAA). Required for the formation of floral organs
CC and vascular tissues. Belongs to the set of redundant YUCCA genes
CC probably responsible for auxin biosynthesis in shoots.
CC {ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:17885085,
CC ECO:0000269|PubMed:22025721, ECO:0000269|PubMed:22986790,
CC ECO:0000269|PubMed:23188833}.
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:0000269|PubMed:17885085, ECO:0000269|PubMed:23188833};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23188833};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for NADPH {ECO:0000269|PubMed:17885085,
CC ECO:0000269|PubMed:23188833};
CC KM=43 uM for phenyl pyruvate {ECO:0000269|PubMed:17885085,
CC ECO:0000269|PubMed:23188833};
CC KM=0.274 mM for tryptamine {ECO:0000269|PubMed:17885085,
CC ECO:0000269|PubMed:23188833};
CC Vmax=9.46 umol/min/mg enzyme with tryptamine as substrate
CC {ECO:0000269|PubMed:17885085, ECO:0000269|PubMed:23188833};
CC Note=kcat is 0.31 sec(-1) for NADPH with phenyl pyruvate as
CC substrate.;
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17885085}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8VZ59-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots but modestly expressed in
CC the cauline leaves and flowers. Expressed in anthers.
CC {ECO:0000269|PubMed:17885085, ECO:0000269|PubMed:18628351}.
CC -!- INDUCTION: Down-regulated by heat stress. Negatively regulated by SPL.
CC {ECO:0000269|PubMed:18557819, ECO:0000269|PubMed:20421476}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC the other members of the YUCCA family. {ECO:0000269|PubMed:16818609}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AC006601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93473.1; -; Genomic_DNA.
DR EMBL; AY065229; AAL38705.1; -; mRNA.
DR EMBL; AY113851; AAM44899.1; -; mRNA.
DR RefSeq; NP_197944.2; NM_122473.3. [Q8VZ59-1]
DR AlphaFoldDB; Q8VZ59; -.
DR SMR; Q8VZ59; -.
DR STRING; 3702.AT5G25620.2; -.
DR PaxDb; Q8VZ59; -.
DR PRIDE; Q8VZ59; -.
DR EnsemblPlants; AT5G25620.1; AT5G25620.1; AT5G25620. [Q8VZ59-1]
DR GeneID; 832638; -.
DR Gramene; AT5G25620.1; AT5G25620.1; AT5G25620. [Q8VZ59-1]
DR KEGG; ath:AT5G25620; -.
DR Araport; AT5G25620; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; Q8VZ59; -.
DR OMA; WRRHYDR; -.
DR PhylomeDB; Q8VZ59; -.
DR BRENDA; 1.14.13.168; 399.
DR UniPathway; UPA00151; -.
DR PRO; PR:Q8VZ59; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZ59; baseline and differential.
DR Genevisible; Q8VZ59; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Auxin biosynthesis; Cytoplasm; FAD; Flavoprotein;
KW Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..417
FT /note="Indole-3-pyruvate monooxygenase YUCCA6"
FT /id="PRO_0000400073"
FT BINDING 36..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 204..209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
SQ SEQUENCE 417 AA; 46638 MW; EE77969BBA647C3B CRC64;
MDFCWKREME GKLAHDHRGM TSPRRICVVT GPVIVGAGPS GLATAACLKE RGITSVLLER
SNCIASLWQL KTYDRLHLHL PKQFCELPII PFPGDFPTYP TKQQFIEYLE DYARRFDIKP
EFNQTVESAA FDENLGMWRV TSVGEEGTTE YVCRWLVAAT GENAEPVVPR FEGMDKFAAA
GVVKHTCHYK TGGDFAGKRV LVVGCGNSGM EVCLDLCNFG AQPSLVVRDA VHVLPREMLG
TSTFGLSMFL LKWLPIRLVD RFLLVVSRFI LGDTTLLGLN RPRLGPLELK NISGKTPVLD
VGTLAKIKTG DIKVCSGIRR LKRHEVEFDN GKTERFDAII LATGYKSNVP SWLKENKMFS
KKDGFPIQEF PEGWRGECGL YAVGFTKRGI SGASMDAKRI AEDIHKCWKQ DEQVKKI
