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Protein

Abscisate beta-glucosyltransferase

Gene

AOG

Organism
Phaseolus angularis (Azuki bean) (Vigna angularis)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Glucosyltransferase involved in the catabolism of abscisic acid (ABA). Adds a glucosyl group at the C-1 position of ABA; (S)-2-trans-abscisate is a better substrate than the natural (+)-S-abscisate or its enantiomer (-)-R-abscisate. No activity with (-)-phaseic acid (PA), methylated-ABA or with other hormones such as jasmonate, zeatin, auxin (IAA) or gibberellin A3 (GA3).1 Publication

Catalytic activityi

UDP-D-glucose + abscisate = UDP + beta-D-glucopyranosyl abscisate.1 Publication

pH dependencei

Optimum pH is 6.0-7.3.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12304.
BRENDAi2.4.1.263. 4737.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Abscisate beta-glucosyltransferase (EC:2.4.1.263)
Alternative name(s):
ABA-glucosyltransferase
Gene namesi
Name:AOG
OrganismiPhaseolus angularis (Azuki bean) (Vigna angularis)
Taxonomic identifieri3914 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Abscisate beta-glucosyltransferasePRO_0000412903Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ8W3P8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Phylogenomic databases

KOiK14595.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8W3P8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLTPSVEI FFFPYVGGGH QIPMIDAARM FASHGASSTI LATPSTTPLF
60 70 80 90 100
QKCITRDQKF GLPISIHTLS ADVPQSDISV GPFLDTSALL EPLRQLLLQR
110 120 130 140 150
RPHCIVVDMF HRWSGDVVYE LGIPRTLFNG IGCFALCVQE NLRHVAFKSV
160 170 180 190 200
STDSEPFLVP NIPDRIEMTM SQLPPFLRNP SGIPERWRGM KQLEEKSFGT
210 220 230 240 250
LINSFYDLEP AYADLIKSKW GNKAWIVGPV SFCNRSKEDK TERGKPPTID
260 270 280 290 300
EQNCLNWLNS KKPSSVLYAS FGSLARLPPE QLKEIAYGLE ASEQSFIWVV
310 320 330 340 350
GNILHNPSEN KENGSGNWLP EGFEQRMKET GKGLVLRGWA PQLLILEHAA
360 370 380 390 400
IKGFMTHCGW NSTLEGVSAG VPMITWPLTA EQFSNEKLIT EVLKTGVQVG
410 420 430 440 450
NREWWPWNAE WKGLVGREKV EVAVRKLMVE SVEADEMRRR AKDIAGKAAR
460 470
AVEEGGTSYA DVEALIQELQ ARTCANQG
Length:478
Mass (Da):53,355
Last modified:March 1, 2002 - v1
Checksum:i901924717EA19F16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB065190 mRNA. Translation: BAB83692.1.

Genome annotation databases

KEGGiag:BAB83692.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB065190 mRNA. Translation: BAB83692.1.

3D structure databases

ProteinModelPortaliQ8W3P8.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAB83692.

Phylogenomic databases

KOiK14595.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12304.
BRENDAi2.4.1.263. 4737.

Family and domain databases

InterProiIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERiPTHR11926. PTHR11926. 1 hit.
PfamiPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEiPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of the abscisic acid-specific glucosyltransferase gene from adzuki bean seedlings."
    Xu Z.J., Nakajima M., Suzuki Y., Yamaguchi I.
    Plant Physiol. 129:1285-1295(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY ABSCISIC ACID; DROUGHT AND WOUNDING, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Hypocotyl.

Entry informationi

Entry nameiAOG_PHAAN
AccessioniPrimary (citable) accession number: Q8W3P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.