ID   AOG_PHAAN               Reviewed;         478 AA.
AC   Q8W3P8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Abscisate beta-glucosyltransferase;
DE            EC=2.4.1.263;
DE   AltName: Full=ABA-glucosyltransferase;
GN   Name=AOG;
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY
RP   ABSCISIC ACID; DROUGHT AND WOUNDING, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Hypocotyl;
RX   PubMed=12114582; DOI=10.1104/pp.001784;
RA   Xu Z.J., Nakajima M., Suzuki Y., Yamaguchi I.;
RT   "Cloning and characterization of the abscisic acid-specific
RT   glucosyltransferase gene from adzuki bean seedlings.";
RL   Plant Physiol. 129:1285-1295(2002).
CC   -!- FUNCTION: Glucosyltransferase involved in the catabolism of abscisic
CC       acid (ABA). Adds a glucosyl group at the C-1 position of ABA; (S)-2-
CC       trans-abscisate is a better substrate than the natural (+)-S-abscisate
CC       or its enantiomer (-)-R-abscisate. No activity with (-)-phaseic acid
CC       (PA), methylated-ABA or with other hormones such as jasmonate, zeatin,
CC       auxin (IAA) or gibberellin A3 (GA3). {ECO:0000269|PubMed:12114582}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-cis-(+)-abscisate + UDP-alpha-D-glucose = beta-D-
CC         glucopyranosyl cis-(+)-abscisate + UDP; Xref=Rhea:RHEA:31031,
CC         ChEBI:CHEBI:22151, ChEBI:CHEBI:37569, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.263;
CC         Evidence={ECO:0000269|PubMed:12114582};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0-7.3. {ECO:0000269|PubMed:12114582};
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB065190; BAB83692.1; -; mRNA.
DR   RefSeq; NP_001316761.1; NM_001329832.1.
DR   AlphaFoldDB; Q8W3P8; -.
DR   SMR; Q8W3P8; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 108341782; -.
DR   KEGG; ag:BAB83692; -.
DR   KEGG; var:108341782; -.
DR   OrthoDB; 508327at2759; -.
DR   BioCyc; MetaCyc:MON-12304; -.
DR   BRENDA; 2.4.1.263; 4737.
DR   GO; GO:0010294; F:abscisic acid glucosyltransferase activity; IEA:RHEA.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..478
FT                   /note="Abscisate beta-glucosyltransferase"
FT                   /id="PRO_0000412903"
SQ   SEQUENCE   478 AA;  53355 MW;  901924717EA19F16 CRC64;
     MKTLTPSVEI FFFPYVGGGH QIPMIDAARM FASHGASSTI LATPSTTPLF QKCITRDQKF
     GLPISIHTLS ADVPQSDISV GPFLDTSALL EPLRQLLLQR RPHCIVVDMF HRWSGDVVYE
     LGIPRTLFNG IGCFALCVQE NLRHVAFKSV STDSEPFLVP NIPDRIEMTM SQLPPFLRNP
     SGIPERWRGM KQLEEKSFGT LINSFYDLEP AYADLIKSKW GNKAWIVGPV SFCNRSKEDK
     TERGKPPTID EQNCLNWLNS KKPSSVLYAS FGSLARLPPE QLKEIAYGLE ASEQSFIWVV
     GNILHNPSEN KENGSGNWLP EGFEQRMKET GKGLVLRGWA PQLLILEHAA IKGFMTHCGW
     NSTLEGVSAG VPMITWPLTA EQFSNEKLIT EVLKTGVQVG NREWWPWNAE WKGLVGREKV
     EVAVRKLMVE SVEADEMRRR AKDIAGKAAR AVEEGGTSYA DVEALIQELQ ARTCANQG