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Indole-3-pyruvate monooxygenase YUCCA6 (EC 1.14.13.168) (Flavin-containing monooxygenase YUCCA6) (Protein HYPERTALL1)

 YUC6_ARATH              Reviewed;         417 AA.
Q8VZ59;
02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
23-MAY-2018, entry version 124.
RecName: Full=Indole-3-pyruvate monooxygenase YUCCA6;
EC=1.14.13.168;
AltName: Full=Flavin-containing monooxygenase YUCCA6;
AltName: Full=Protein HYPERTALL1;
Name=YUC6; Synonyms=HYT1, YUCCA6; OrderedLocusNames=At5g25620;
ORFNames=T14C9.160;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
FUNCTION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
PubMed=16818609; DOI=10.1101/gad.1415106;
Cheng Y., Dai X., Zhao Y.;
"Auxin biosynthesis by the YUCCA flavin monooxygenases controls the
formation of floral organs and vascular tissues in Arabidopsis.";
Genes Dev. 20:1790-1799(2006).
[5]
GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=17461789; DOI=10.1111/j.1365-313X.2007.03101.x;
Hansen B.G., Kliebenstein D.J., Halkier B.A.;
"Identification of a flavin-monooxygenase as the S-oxygenating enzyme
in aliphatic glucosinolate biosynthesis in Arabidopsis.";
Plant J. 50:902-910(2007).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=17885085; DOI=10.1104/pp.107.104935;
Kim J.I., Sharkhuu A., Jin J.B., Li P., Jeong J.C., Baek D., Lee S.Y.,
Blakeslee J.J., Murphy A.S., Bohnert H.J., Hasegawa P.M., Yun D.J.,
Bressan R.A.;
"yucca6, a dominant mutation in Arabidopsis, affects auxin
accumulation and auxin-related phenotypes.";
Plant Physiol. 145:722-735(2007).
[7]
INDUCTION BY SPL.
PubMed=18557819; DOI=10.1111/j.1469-8137.2008.02514.x;
Li L.C., Qin G.J., Tsuge T., Hou X.H., Ding M.Y., Aoyama T., Oka A.,
Chen Z., Gu H., Zhao Y., Qu L.J.;
"SPOROCYTELESS modulates YUCCA expression to regulate the development
of lateral organs in Arabidopsis.";
New Phytol. 179:751-764(2008).
[8]
TISSUE SPECIFICITY.
PubMed=18628351; DOI=10.1105/tpc.107.057570;
Cecchetti V., Altamura M.M., Falasca G., Costantino P., Cardarelli M.;
"Auxin regulates Arabidopsis anther dehiscence, pollen maturation, and
filament elongation.";
Plant Cell 20:1760-1774(2008).
[9]
INDUCTION BY HEAT.
PubMed=20421476; DOI=10.1073/pnas.1000869107;
Sakata T., Oshino T., Miura S., Tomabechi M., Tsunaga Y.,
Higashitani N., Miyazawa Y., Takahashi H., Watanabe M.,
Higashitani A.;
"Auxins reverse plant male sterility caused by high temperatures.";
Proc. Natl. Acad. Sci. U.S.A. 107:8569-8574(2010).
[10]
FUNCTION.
PubMed=22025721; DOI=10.1073/pnas.1108436108;
Won C., Shen X., Mashiguchi K., Zheng Z., Dai X., Cheng Y.,
Kasahara H., Kamiya Y., Chory J., Zhao Y.;
"Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN
AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 108:18518-18523(2011).
[11]
FUNCTION.
PubMed=22986790; DOI=10.1093/mp/sss100;
Kim J.I., Baek D., Park H.C., Chun H.J., Oh D.H., Lee M.K., Cha J.Y.,
Kim W.Y., Kim M.C., Chung W.S., Bohnert H.J., Lee S.Y., Bressan R.A.,
Lee S.W., Yun D.J.;
"Overexpression of Arabidopsis YUCCA6 in potato results in high-auxin
developmental phenotypes and enhanced resistance to water deficit.";
Mol. Plant 6:337-349(2013).
[12]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=23188833; DOI=10.1074/jbc.M112.424077;
Dai X., Mashiguchi K., Chen Q., Kasahara H., Kamiya Y., Ojha S.,
Dubois J., Ballou D., Zhao Y.;
"The biochemical mechanism of auxin biosynthesis by an Arabidopsis
YUCCA flavin-containing monooxygenase.";
J. Biol. Chem. 288:1448-1457(2013).
-!- FUNCTION: Involved in auxin biosynthesis via the indole-3-pyruvic
acid (IPA) pathway. Also able to convert in vitro phenyl pyruvate
(PPA) to phenyl acetic acid (PAA). Required for the formation of
floral organs and vascular tissues. Belongs to the set of
redundant YUCCA genes probably responsible for auxin biosynthesis
in shoots. {ECO:0000269|PubMed:16818609,
ECO:0000269|PubMed:17885085, ECO:0000269|PubMed:22025721,
ECO:0000269|PubMed:22986790, ECO:0000269|PubMed:23188833}.
-!- CATALYTIC ACTIVITY: (Indol-3-yl)pyruvate + NADPH + O(2) = (indol-
3-yl)acetate + NADP(+) + H(2)O + CO(2).
{ECO:0000269|PubMed:17885085, ECO:0000269|PubMed:23188833}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:23188833};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=26 uM for NADPH {ECO:0000269|PubMed:17885085,
ECO:0000269|PubMed:23188833};
KM=43 uM for phenyl pyruvate {ECO:0000269|PubMed:17885085,
ECO:0000269|PubMed:23188833};
KM=0.274 mM for tryptamine {ECO:0000269|PubMed:17885085,
ECO:0000269|PubMed:23188833};
Vmax=9.46 umol/min/mg enzyme with tryptamine as substrate
{ECO:0000269|PubMed:17885085, ECO:0000269|PubMed:23188833};
Note=kcat is 0.31 sec(-1) for NADPH with phenyl pyruvate as
substrate.;
-!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17885085}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q8VZ59-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Highly expressed in roots but modestly
expressed in the cauline leaves and flowers. Expressed in anthers.
{ECO:0000269|PubMed:17885085, ECO:0000269|PubMed:18628351}.
-!- INDUCTION: Down-regulated by heat stress. Negatively regulated by
SPL. {ECO:0000269|PubMed:18557819, ECO:0000269|PubMed:20421476}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy
with the other members of the YUCCA family.
{ECO:0000269|PubMed:16818609}.
-!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC006601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED93473.1; -; Genomic_DNA.
EMBL; AY065229; AAL38705.1; -; mRNA.
EMBL; AY113851; AAM44899.1; -; mRNA.
RefSeq; NP_197944.2; NM_122473.3. [Q8VZ59-1]
UniGene; At.28557; -.
ProteinModelPortal; Q8VZ59; -.
SMR; Q8VZ59; -.
STRING; 3702.AT5G25620.2; -.
PaxDb; Q8VZ59; -.
EnsemblPlants; AT5G25620.1; AT5G25620.1; AT5G25620. [Q8VZ59-1]
GeneID; 832638; -.
Gramene; AT5G25620.1; AT5G25620.1; AT5G25620. [Q8VZ59-1]
KEGG; ath:AT5G25620; -.
Araport; AT5G25620; -.
eggNOG; KOG1399; Eukaryota.
eggNOG; COG2072; LUCA.
HOGENOM; HOG000240759; -.
InParanoid; Q8VZ59; -.
KO; K11816; -.
PhylomeDB; Q8VZ59; -.
BRENDA; 1.14.13.168; 399.
Reactome; R-ATH-217271; FMO oxidises nucleophiles.
UniPathway; UPA00151; -.
PRO; PR:Q8VZ59; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8VZ59; baseline and differential.
Genevisible; Q8VZ59; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR000960; Flavin_mOase.
InterPro; IPR020946; Flavin_mOase-like.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Pfam; PF00743; FMO-like; 1.
PIRSF; PIRSF000332; FMO; 1.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51735; SSF51735; 2.
SUPFAM; SSF51905; SSF51905; 1.
1: Evidence at protein level;
Alternative splicing; Auxin biosynthesis; Complete proteome;
Cytoplasm; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
Reference proteome.
CHAIN 1 417 Indole-3-pyruvate monooxygenase YUCCA6.
/FTId=PRO_0000400073.
NP_BIND 36 41 FAD. {ECO:0000255}.
NP_BIND 204 209 NADP. {ECO:0000255}.
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


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