Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Probable indole-3-pyruvate monooxygenase YUCCA1 (EC 1.14.13.168) (Flavin-containing monooxygenase YUCCA1)

 YUC1_ARATH              Reviewed;         414 AA.
Q9SZY8;
02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 128.
RecName: Full=Probable indole-3-pyruvate monooxygenase YUCCA1;
EC=1.14.13.168;
AltName: Full=Flavin-containing monooxygenase YUCCA1;
Name=YUC1; Synonyms=YUC, YUCCA, YUCCA1; OrderedLocusNames=At4g32540;
ORFNames=L23H3.20;
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 [GENOMIC DNA], AND FUNCTION.
PubMed=11209081; DOI=10.1126/science.291.5502.306;
Zhao Y., Christensen S.K., Fankhauser C., Cashman J.R., Cohen J.D.,
Weigel D., Chory J.;
"A role for flavin monooxygenase-like enzymes in auxin biosynthesis.";
Science 291:306-309(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
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).
[4]
GENE FAMILY, NOMENCLATURE, FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
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]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=17704214; DOI=10.1105/tpc.107.053009;
Cheng Y., Dai X., Zhao Y.;
"Auxin synthesized by the YUCCA flavin monooxygenases is essential for
embryogenesis and leaf formation in Arabidopsis.";
Plant Cell 19:2430-2439(2007).
[6]
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).
[7]
FUNCTION.
PubMed=20974893; DOI=10.1104/pp.110.165803;
Tivendale N.D., Davies N.W., Molesworth P.P., Davidson S.E.,
Smith J.A., Lowe E.K., Reid J.B., Ross J.J.;
"Reassessing the role of N-hydroxytryptamine in auxin biosynthesis.";
Plant Physiol. 154:1957-1965(2010).
[8]
FUNCTION, MUTAGENESIS OF GLY-25; GLY-30; SER-139 AND GLY-194, AND
DISRUPTION PHENOTYPE.
PubMed=21205174; DOI=10.1111/j.1744-7909.2010.01007.x;
Hou X., Liu S., Pierri F., Dai X., Qu L.J., Zhao Y.;
"Allelic analyses of the Arabidopsis YUC1 locus reveal residues and
domains essential for the functions of YUC family of flavin
monooxygenases.";
J. Integr. Plant Biol. 53:54-62(2011).
[9]
FUNCTION.
PubMed=22108406; DOI=10.1105/tpc.111.088047;
Stepanova A.N., Yun J., Robles L.M., Novak O., He W., Guo H.,
Ljung K., Alonso J.M.;
"The Arabidopsis YUCCA1 flavin monooxygenase functions in the indole-
3-pyruvic acid branch of auxin biosynthesis.";
Plant Cell 23:3961-3973(2011).
[10]
FUNCTION.
PubMed=21358284; DOI=10.4161/psb.6.3.14450;
Ross J.J., Tivendale N.D., Reid J.B., Davies N.W., Molesworth P.P.,
Lowe E.K., Smith J.A., Davidson S.E.;
"Reassessing the role of YUCCAs in auxin biosynthesis.";
Plant Signal. Behav. 6:437-439(2011).
[11]
FUNCTION.
PubMed=22025724; DOI=10.1073/pnas.1108434108;
Mashiguchi K., Tanaka K., Sakai T., Sugawara S., Kawaide H.,
Natsume M., Hanada A., Yaeno T., Shirasu K., Yao H., McSteen P.,
Zhao Y., Hayashi K., Kamiya Y., Kasahara H.;
"The main auxin biosynthesis pathway in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 108:18512-18517(2011).
[12]
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).
-!- FUNCTION: Involved in auxin biosynthesis, but not in the
tryptamine or the CYP79B2/B3 branches. Catalyzes in vitro the N-
oxidation of tryptamine to form N-hydroxyl tryptamine. Involved
during embryogenesis and seedling development. 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:11209081,
ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:17704214,
ECO:0000269|PubMed:20974893, ECO:0000269|PubMed:21205174,
ECO:0000269|PubMed:21358284, ECO:0000269|PubMed:22025721,
ECO:0000269|PubMed:22025724, ECO:0000269|PubMed:22108406}.
-!- CATALYTIC ACTIVITY: (Indol-3-yl)pyruvate + NADPH + O(2) = (indol-
3-yl)acetate + NADP(+) + H(2)O + CO(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
-!- TISSUE SPECIFICITY: Expressed in the apical meristems and young
floral primordia. Detected in the floral meristems and at the base
of the floral organs. {ECO:0000269|PubMed:16818609}.
-!- DEVELOPMENTAL STAGE: Expression relatively broad during early
stages of embryogenesis and more restricted to discrete groups of
cells in mature embryos. Later, expression mainly restricted to
the cotyledons and the apical meristem.
{ECO:0000269|PubMed:17704214}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy
with the other members of the YUCCA family.
{ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:21205174}.
-!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
-!- CAUTION: Was initially (PubMed:11209081) thought to be involved in
the tryptamine pathway for the biosynthesis of indole-3-acetic
acid (IAA), but it has been shown (PubMed:20974893) that this is
not the case. It is now admitted (PubMed:22025724 and
PubMed:22108406) that the YUCCA family is implicated in the
conversion of indole-3-pyruvic acid (IPA) to indole-3-acetic acid
(IAA). {ECO:0000305|PubMed:11209081, ECO:0000305|PubMed:20974893}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY057102; AAL23750.1; -; Genomic_DNA.
EMBL; AL050398; CAB43691.1; -; Genomic_DNA.
EMBL; AL161581; CAB79971.1; -; Genomic_DNA.
EMBL; CP002687; AEE86075.1; -; Genomic_DNA.
PIR; T08587; T08587.
RefSeq; NP_194980.1; NM_119406.3.
UniGene; At.54581; -.
ProteinModelPortal; Q9SZY8; -.
SMR; Q9SZY8; -.
STRING; 3702.AT4G32540.1; -.
PaxDb; Q9SZY8; -.
PRIDE; Q9SZY8; -.
EnsemblPlants; AT4G32540.1; AT4G32540.1; AT4G32540.
GeneID; 829389; -.
Gramene; AT4G32540.1; AT4G32540.1; AT4G32540.
KEGG; ath:AT4G32540; -.
Araport; AT4G32540; -.
TAIR; locus:2131322; AT4G32540.
eggNOG; KOG1399; Eukaryota.
eggNOG; COG2072; LUCA.
HOGENOM; HOG000240759; -.
InParanoid; Q9SZY8; -.
KO; K11816; -.
OMA; FRNQRVL; -.
OrthoDB; EOG09360B3O; -.
PhylomeDB; Q9SZY8; -.
BRENDA; 1.14.13.168; 399.
Reactome; R-ATH-217271; FMO oxidises nucleophiles.
UniPathway; UPA00151; -.
PRO; PR:Q9SZY8; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SZY8; differential.
Genevisible; Q9SZY8; AT.
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; IMP:TAIR.
GO; GO:0048825; P:cotyledon development; IGI:TAIR.
GO; GO:0010229; P:inflorescence development; IGI:TAIR.
GO; GO:0048827; P:phyllome development; IGI:TAIR.
GO; GO:0009911; P:positive regulation of flower development; IGI:TAIR.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR020946; Flavin_mOase-like.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
Pfam; PF00743; FMO-like; 1.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
Auxin biosynthesis; Complete proteome; FAD; Flavoprotein;
Monooxygenase; NADP; Oxidoreductase; Reference proteome.
CHAIN 1 414 Probable indole-3-pyruvate monooxygenase
YUCCA1.
/FTId=PRO_0000400068.
NP_BIND 25 30 FAD. {ECO:0000255}.
NP_BIND 189 194 NADP. {ECO:0000255}.
MUTAGEN 25 25 G->E: In yuc1-4; loss of activity.
{ECO:0000269|PubMed:21205174}.
MUTAGEN 30 30 G->D: In yuc1-5; loss of activity.
{ECO:0000269|PubMed:21205174}.
MUTAGEN 139 139 S->F: In yuc1-7; loss of activity.
{ECO:0000269|PubMed:21205174}.
MUTAGEN 194 194 G->D: In yuc1-6; loss of activity.
{ECO:0000269|PubMed:21205174}.
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


Related products :

Catalog number Product name Quantity
GTX104172 flavin containing monooxygenase 1 100 µg
YF-PA11827 anti-Flavin containing monooxygenase 4 50 ul
orb74118 Flavin containing monooxygenase 1 antibody 100 ul
FMO3 FMO1 Gene flavin containing monooxygenase 1
E11846h Human Flavin Containing Monooxygenase 3 ELISA Kit 96T
E11845h Human Flavin Containing Monooxygenase 4 ELISA Kit 96T
NBL1-10777 Flavin containing monooxygenase 4 Lysate 0.1 mg
E9695h Human Flavin Containing Monooxygenase 2, Non Funct 96T
E11847h Human Flavin Containing Monooxygenase 1 ELISA Kit 96T
FMR1 FMO5 Gene flavin containing monooxygenase 5
FMOD FMO4 Gene flavin containing monooxygenase 4
P3135Rb Rabbit anti_ flavin containing monooxygenase 5 pol 40ug/0.2ml
201-20-2081 FMO3{flavin containing monooxygenase 3}rabbit.pAb 0.2ml
FMO5 FMO3 Gene flavin containing monooxygenase 3
201-20-2083 FMO5{flavin containing monooxygenase 5}rabbit.pAb 0.2ml
201-20-2082 FMO4{flavin containing monooxygenase 4}rabbit.pAb 0.2ml
201-20-2080 FMO2{flavin containing monooxygenase 2 (non-functional)}rabbit.pAb 0.2ml
E1380135 Guinea pig Flavin Containing Monooxygenase 5 (FMO5) ELISA Kit
201-20-0020 FMO2{flavin containing monooxygenase 2 (non-functional)}goat.pAb 0.2ml
FMO4 FMO2 Gene flavin containing monooxygenase 2 (non-functional)
GWB-9D4DF9 Anti- FMO3 (flavin containing monooxygenase 3) Antibody
SEF458Hu ELISA Kit for Flavin Containing Monooxygenase 1 (FMO1) Homo sapiens (Human) 96T
22997 flavin containing monooxygenase 1 antibody, Rabbit Polyconal Ab, Species Reactivity: Human 100
YF-PA11827 anti-Flavin containing monooxygenase 4 type: Primary antibodies host: Mouse 50 ul
CSB-EL008749RA Rat flavin containing monooxygenase 3 (FMO3) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur