YUC1_ARATH
ID YUC1_ARATH Reviewed; 414 AA.
AC Q9SZY8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable indole-3-pyruvate monooxygenase YUCCA1;
DE EC=1.14.13.168;
DE AltName: Full=Flavin-containing monooxygenase YUCCA1;
GN Name=YUC1; Synonyms=YUC, YUCCA, YUCCA1; OrderedLocusNames=At4g32540;
GN ORFNames=L23H3.20;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=11209081; DOI=10.1126/science.291.5502.306;
RA Zhao Y., Christensen S.K., Fankhauser C., Cashman J.R., Cohen J.D.,
RA Weigel D., Chory J.;
RT "A role for flavin monooxygenase-like enzymes in auxin biosynthesis.";
RL Science 291:306-309(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 GENE FAMILY, NOMENCLATURE, FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
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 FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17704214; DOI=10.1105/tpc.107.053009;
RA Cheng Y., Dai X., Zhao Y.;
RT "Auxin synthesized by the YUCCA flavin monooxygenases is essential for
RT embryogenesis and leaf formation in Arabidopsis.";
RL Plant Cell 19:2430-2439(2007).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=20974893; DOI=10.1104/pp.110.165803;
RA Tivendale N.D., Davies N.W., Molesworth P.P., Davidson S.E., Smith J.A.,
RA Lowe E.K., Reid J.B., Ross J.J.;
RT "Reassessing the role of N-hydroxytryptamine in auxin biosynthesis.";
RL Plant Physiol. 154:1957-1965(2010).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLY-25; GLY-30; SER-139 AND GLY-194, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21205174; DOI=10.1111/j.1744-7909.2010.01007.x;
RA Hou X., Liu S., Pierri F., Dai X., Qu L.J., Zhao Y.;
RT "Allelic analyses of the Arabidopsis YUC1 locus reveal residues and domains
RT essential for the functions of YUC family of flavin monooxygenases.";
RL J. Integr. Plant Biol. 53:54-62(2011).
RN [9]
RP FUNCTION.
RX PubMed=22108406; DOI=10.1105/tpc.111.088047;
RA Stepanova A.N., Yun J., Robles L.M., Novak O., He W., Guo H., Ljung K.,
RA Alonso J.M.;
RT "The Arabidopsis YUCCA1 flavin monooxygenase functions in the indole-3-
RT pyruvic acid branch of auxin biosynthesis.";
RL Plant Cell 23:3961-3973(2011).
RN [10]
RP FUNCTION.
RX PubMed=21358284; DOI=10.4161/psb.6.3.14450;
RA Ross J.J., Tivendale N.D., Reid J.B., Davies N.W., Molesworth P.P.,
RA Lowe E.K., Smith J.A., Davidson S.E.;
RT "Reassessing the role of YUCCAs in auxin biosynthesis.";
RL Plant Signal. Behav. 6:437-439(2011).
RN [11]
RP FUNCTION.
RX PubMed=22025724; DOI=10.1073/pnas.1108434108;
RA Mashiguchi K., Tanaka K., Sakai T., Sugawara S., Kawaide H., Natsume M.,
RA Hanada A., Yaeno T., Shirasu K., Yao H., McSteen P., Zhao Y., Hayashi K.,
RA Kamiya Y., Kasahara H.;
RT "The main auxin biosynthesis pathway in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18512-18517(2011).
RN [12]
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).
CC -!- FUNCTION: Involved in auxin biosynthesis, but not in the tryptamine or
CC the CYP79B2/B3 branches. Catalyzes in vitro the N-oxidation of
CC tryptamine to form N-hydroxyl tryptamine. Involved during embryogenesis
CC and seedling development. 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:11209081, ECO:0000269|PubMed:16818609,
CC ECO:0000269|PubMed:17704214, ECO:0000269|PubMed:20974893,
CC ECO:0000269|PubMed:21205174, ECO:0000269|PubMed:21358284,
CC ECO:0000269|PubMed:22025721, ECO:0000269|PubMed:22025724,
CC ECO:0000269|PubMed:22108406}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in the apical meristems and young floral
CC primordia. Detected in the floral meristems and at the base of the
CC floral organs. {ECO:0000269|PubMed:16818609}.
CC -!- DEVELOPMENTAL STAGE: Expression relatively broad during early stages of
CC embryogenesis and more restricted to discrete groups of cells in mature
CC embryos. Later, expression mainly restricted to the cotyledons and the
CC apical meristem. {ECO:0000269|PubMed:17704214}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC the other members of the YUCCA family. {ECO:0000269|PubMed:16818609,
CC ECO:0000269|PubMed:21205174}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
CC -!- CAUTION: Was initially (PubMed:11209081) thought to be involved in the
CC tryptamine pathway for the biosynthesis of indole-3-acetic acid (IAA),
CC but it has been shown (PubMed:20974893) that this is not the case. It
CC is now admitted (PubMed:22025724 and PubMed:22108406) that the YUCCA
CC family is implicated in the conversion of indole-3-pyruvic acid (IPA)
CC to indole-3-acetic acid (IAA). {ECO:0000305|PubMed:11209081,
CC ECO:0000305|PubMed:20974893}.
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DR EMBL; AY057102; AAL23750.1; -; Genomic_DNA.
DR EMBL; AL050398; CAB43691.1; -; Genomic_DNA.
DR EMBL; AL161581; CAB79971.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86075.1; -; Genomic_DNA.
DR PIR; T08587; T08587.
DR RefSeq; NP_194980.1; NM_119406.3.
DR AlphaFoldDB; Q9SZY8; -.
DR SMR; Q9SZY8; -.
DR STRING; 3702.AT4G32540.1; -.
DR PaxDb; Q9SZY8; -.
DR EnsemblPlants; AT4G32540.1; AT4G32540.1; AT4G32540.
DR GeneID; 829389; -.
DR Gramene; AT4G32540.1; AT4G32540.1; AT4G32540.
DR KEGG; ath:AT4G32540; -.
DR Araport; AT4G32540; -.
DR TAIR; locus:2131322; AT4G32540.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_2_0_1; -.
DR InParanoid; Q9SZY8; -.
DR OMA; MIQIMEG; -.
DR PhylomeDB; Q9SZY8; -.
DR BRENDA; 1.14.13.168; 399.
DR UniPathway; UPA00151; -.
DR PRO; PR:Q9SZY8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZY8; baseline and differential.
DR Genevisible; Q9SZY8; AT.
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; IMP:TAIR.
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 1: Evidence at protein level;
KW Auxin biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..414
FT /note="Probable indole-3-pyruvate monooxygenase YUCCA1"
FT /id="PRO_0000400068"
FT BINDING 25..30
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 189..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT MUTAGEN 25
FT /note="G->E: In yuc1-4; loss of activity."
FT /evidence="ECO:0000269|PubMed:21205174"
FT MUTAGEN 30
FT /note="G->D: In yuc1-5; loss of activity."
FT /evidence="ECO:0000269|PubMed:21205174"
FT MUTAGEN 139
FT /note="S->F: In yuc1-7; loss of activity."
FT /evidence="ECO:0000269|PubMed:21205174"
FT MUTAGEN 194
FT /note="G->D: In yuc1-6; loss of activity."
FT /evidence="ECO:0000269|PubMed:21205174"
SQ SEQUENCE 414 AA; 46018 MW; 3BAF7A909C4A07E8 CRC64;
MESHPHNKTD QTQHIILVHG PIIIGAGPSG LATSACLSSR GVPSLILERS DSIASLWKSK
TYDRLRLHLP KHFCRLPLLD FPEYYPKYPS KNEFLAYLES YASHFRIAPR FNKNVQNAAY
DSSSGFWRVK THDNTEYLSK WLIVATGENA DPYFPEIPGR KKFSGGKIVH ASEYKSGEEF
RRQKVLVVGC GNSGMEISLD LVRHNASPHL VVRNTVHVLP REILGVSTFG VGMTLLKCLP
LRLVDKFLLL MANLSFGNTD RLGLRRPKTG PLELKNVTGK SPVLDVGAMS LIRSGMIQIM
EGVKEITKKG AKFMDGQEKD FDSIIFATGY KSNVPTWLQG GDFFTDDGMP KTPFPNGWRG
GKGLYTVGFT RRGLLGTASD AVKIAGEIGD QWRDEIKGST RNMCSSRFVF TSKS
