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UDP-glycosyltransferase 75B1 (EC 2.4.1.-) ((Uridine 5'-diphosphate-glucose:indol-3-ylacetyl)-beta-D-glucosyl transferase 1) (IAA-Glu synthase 1) (Indole-3-acetate beta-glucosyltransferase 1) (EC 2.4.1.121)

 U75B1_ARATH             Reviewed;         469 AA.
Q9LR44;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 115.
RecName: Full=UDP-glycosyltransferase 75B1;
EC=2.4.1.-;
AltName: Full=(Uridine 5'-diphosphate-glucose:indol-3-ylacetyl)-beta-D-glucosyl transferase 1;
AltName: Full=IAA-Glu synthase 1;
AltName: Full=Indole-3-acetate beta-glucosyltransferase 1;
EC=2.4.1.121;
Name=UGT75B1; Synonyms=UGT1; OrderedLocusNames=At1g05560;
ORFNames=T25N20.20;
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 [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
CALS1; ROP1 AND PHRAGMOPLASTIN.
STRAIN=cv. Columbia;
PubMed=11283335; DOI=10.1105/tpc.13.4.769;
Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
"A novel UDP-glucose transferase is part of the callose synthase
complex and interacts with phragmoplastin at the forming cell plate.";
Plant Cell 13:769-779(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[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]
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).
[5]
GENE FAMILY.
PubMed=11042215; DOI=10.1074/jbc.M007447200;
Li Y., Baldauf S., Lim E.K., Bowles D.J.;
"Phylogenetic analysis of the UDP-glycosyltransferase multigene family
of Arabidopsis thaliana.";
J. Biol. Chem. 276:4338-4343(2001).
[6]
FUNCTION.
PubMed=11042207; DOI=10.1074/jbc.M006185200;
Jackson R.G., Lim E.-K., Li Y., Kowalczyk M., Sandberg G., Hoggett J.,
Ashford D.A., Bowles D.J.;
"Identification and biochemical characterization of an Arabidopsis
indole-3-acetic acid glucosyltransferase.";
J. Biol. Chem. 276:4350-4356(2001).
[7]
FUNCTION.
PubMed=11641410; DOI=10.1074/jbc.M109287200;
Lim E.K., Doucet C.J., Li Y., Elias L., Worrall D., Spencer S.P.,
Ross J., Bowles D.J.;
"The activity of Arabidopsis glycosyltransferases toward salicylic
acid, 4-hydroxybenzoic acid, and other benzoates.";
J. Biol. Chem. 277:586-592(2002).
[8]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=18385129; DOI=10.1074/jbc.M709591200;
Eudes A., Bozzo G.G., Waller J.C., Naponelli V., Lim E.K.,
Bowles D.J., Gregory J.F. III, Hanson A.D.;
"Metabolism of the folate precursor p-aminobenzoate in plants: glucose
ester formation and vacuolar storage.";
J. Biol. Chem. 283:15451-15459(2008).
-!- FUNCTION: Possesses low catalytic activity on indole-3-acetic acid
(IAA) in vitro. May transfer UDP-glucose from sucrose synthase to
callose synthase for the synthesis of callose at the forming cell
plate during cytokinesis. Has high affinity for 4-aminobenzoate.
Catalyzes the formation of 4-aminobenzoate glucose ester which
represents a storage form of 4-aminobenzoate in the vacuole. Is
the major source of this activity in the plant. Also active in
vitro on benzoates and benzoate derivatives.
{ECO:0000269|PubMed:11042207, ECO:0000269|PubMed:11641410,
ECO:0000269|PubMed:18385129}.
-!- CATALYTIC ACTIVITY: UDP-glucose + (indol-3-yl)acetate = UDP + 1-O-
(indol-3-yl)acetyl-beta-D-glucose.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=120 uM for 4-aminobenzoate {ECO:0000269|PubMed:18385129};
-!- PATHWAY: Plant hormone metabolism; auxin conjugation.
-!- SUBUNIT: Interacts with CALS1, ROP1 and phragmoplastin.
{ECO:0000269|PubMed:11283335}.
-!- INTERACTION:
Q39821:- (xeno); NbExp=2; IntAct=EBI-1765823, EBI-1765815;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:11283335}. Cytoplasm, cytoskeleton,
phragmoplast {ECO:0000269|PubMed:11283335}. Note=During
interphase, distributed in a punctate pattern in the perinuclear
region. Localized in the forming cell plate during cytokinesis.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
condition, but strong reduction in 4-aminobenzoate
glucosyltransferase activity. {ECO:0000269|PubMed:18385129}.
-!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF196777; AAK37839.1; -; mRNA.
EMBL; AC005106; AAF79730.1; -; Genomic_DNA.
EMBL; CP002684; AEE27854.1; -; Genomic_DNA.
EMBL; AF367358; AAK32944.1; -; mRNA.
EMBL; AY078051; AAL77752.1; -; mRNA.
RefSeq; NP_563742.1; NM_100435.3.
UniGene; At.20182; -.
ProteinModelPortal; Q9LR44; -.
SMR; Q9LR44; -.
BioGrid; 22300; 1.
IntAct; Q9LR44; 3.
STRING; 3702.AT1G05560.1; -.
CAZy; GT1; Glycosyltransferase Family 1.
PaxDb; Q9LR44; -.
PRIDE; Q9LR44; -.
EnsemblPlants; AT1G05560.1; AT1G05560.1; AT1G05560.
EnsemblPlants; AT1G05560.2; AT1G05560.2; AT1G05560.
GeneID; 837058; -.
Gramene; AT1G05560.1; AT1G05560.1; AT1G05560.
Gramene; AT1G05560.2; AT1G05560.2; AT1G05560.
KEGG; ath:AT1G05560; -.
Araport; AT1G05560; -.
TAIR; locus:2201031; AT1G05560.
eggNOG; KOG1192; Eukaryota.
eggNOG; COG1819; LUCA.
HOGENOM; HOG000237567; -.
InParanoid; Q9LR44; -.
KO; K13692; -.
OMA; VTCVSVF; -.
OrthoDB; EOG09360B34; -.
PhylomeDB; Q9LR44; -.
BioCyc; ARA:AT1G05560-MONOMER; -.
BioCyc; MetaCyc:AT1G05560-MONOMER; -.
UniPathway; UPA00376; -.
PRO; PR:Q9LR44; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9LR44; differential.
Genevisible; Q9LR44; AT.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0047215; F:indole-3-acetate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
GO; GO:0080002; F:UDP-glucose:4-aminobenzoate acylglucosyltransferase activity; IDA:TAIR.
GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
GO; GO:0008194; F:UDP-glycosyltransferase activity; ISS:TAIR.
GO; GO:0009920; P:cell plate formation involved in plant-type cell wall biogenesis; TAS:TAIR.
GO; GO:0046482; P:para-aminobenzoic acid metabolic process; IDA:TAIR.
GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
InterPro; IPR002213; UDP_glucos_trans.
InterPro; IPR035595; UDP_glycos_trans_CS.
Pfam; PF00201; UDPGT; 1.
PROSITE; PS00375; UDPGT; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Glycosyltransferase;
Reference proteome; Transferase.
CHAIN 1 469 UDP-glycosyltransferase 75B1.
/FTId=PRO_0000334597.
REGION 332 334 UDP-glucose binding. {ECO:0000250}.
REGION 349 357 UDP-glucose binding. {ECO:0000250}.
REGION 371 374 UDP-glucose binding. {ECO:0000250}.
BINDING 267 267 UDP-glucose. {ECO:0000250}.
SEQUENCE 469 AA; 52813 MW; 77C6088342C78D76 CRC64;
MAPPHFLLVT FPAQGHVNPS LRFARRLIKR TGARVTFVTC VSVFHNSMIA NHNKVENLSF
LTFSDGFDDG GISTYEDRQK RSVNLKVNGD KALSDFIEAT KNGDSPVTCL IYTILLNWAP
KVARRFQLPS ALLWIQPALV FNIYYTHFMG NKSVFELPNL SSLEIRDLPS FLTPSNTNKG
AYDAFQEMME FLIKETKPKI LINTFDSLEP EALTAFPNID MVAVGPLLPT EIFSGSTNKS
VKDQSSSYTL WLDSKTESSV IYVSFGTMVE LSKKQIEELA RALIEGKRPF LWVITDKSNR
ETKTEGEEET EIEKIAGFRH ELEEVGMIVS WCSQIEVLSH RAVGCFVTHC GWSSTLESLV
LGVPVVAFPM WSDQPTNAKL LEESWKTGVR VRENKDGLVE RGEIRRCLEA VMEEKSVELR
ENAKKWKRLA MEAGREGGSS DKNMEAFVED ICGESLIQNL CEAEEVKVK


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