ANGT_GENTR
ID ANGT_GENTR Reviewed; 482 AA.
AC Q8H0F2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Anthocyanin 3'-O-beta-glucosyltransferase;
DE Short=3'GT;
DE EC=2.4.1.238;
OS Gentiana triflora (Clustered gentian).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Gentianaceae; Gentianeae; Gentianinae;
OC Gentiana.
OX NCBI_TaxID=55190;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 109-130; 182-186; 203-211;
RP 347-365 AND 457-471, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Japonica;
RX PubMed=12857844; DOI=10.1104/pp.102.018242;
RA Fukuchi-Mizutani M., Okuhara H., Fukui Y., Nakao M., Katsumoto Y.,
RA Yonekura-Sakakibara K., Kusumi T., Hase T., Tanaka Y.;
RT "Biochemical and molecular characterization of a novel UDP-
RT glucose:anthocyanin 3'-O-glucosyltransferase, a key enzyme for blue
RT anthocyanin biosynthesis, from gentian.";
RL Plant Physiol. 132:1652-1663(2003).
CC -!- FUNCTION: Specifically glucosylates the 3'-hydroxy group of delphinidin
CC 3,5-di-O-glucoside to produce gentiodelphin. Shows a strict specificity
CC for UDP-glucose as donor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delphinidin 3,5-bis-O-beta-D-glucoside + UDP-alpha-D-glucose =
CC delphinidin 3,3',5-tri-O-beta-D-glucoside + H(+) + UDP;
CC Xref=Rhea:RHEA:35627, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:77838, ChEBI:CHEBI:77844;
CC EC=2.4.1.238;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for delphinidin 3,5-di-O-glucoside
CC {ECO:0000269|PubMed:12857844};
CC Vmax=1370 nmol/min/mg enzyme {ECO:0000269|PubMed:12857844};
CC -!- TISSUE SPECIFICITY: Abundant in petals and barely detected in leaves.
CC {ECO:0000269|PubMed:12857844}.
CC -!- DEVELOPMENTAL STAGE: Expressed early in petals development and
CC decreases in fully opened flowers. {ECO:0000269|PubMed:12857844}.
CC -!- INDUCTION: Significantly inhibited by Al(3+) and Co(2+), moderately by
CC Zn(2+) and not by Mg(2+), Ca(2+), Mn(2+), EDAT or EGTA. Competitively
CC inhibited by UDP. {ECO:0000269|PubMed:12857844}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB076697; BAC54092.1; -; mRNA.
DR AlphaFoldDB; Q8H0F2; -.
DR SMR; Q8H0F2; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR KEGG; ag:BAC54092; -.
DR BRENDA; 2.4.1.238; 2412.
DR SABIO-RK; Q8H0F2; -.
DR GO; GO:0033837; F:anthocyanin 3'-O-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosyltransferase; Transferase.
FT CHAIN 1..482
FT /note="Anthocyanin 3'-O-beta-glucosyltransferase"
FT /id="PRO_0000310729"
SQ SEQUENCE 482 AA; 54041 MW; BDBC12F21C7F7147 CRC64;
MDQLHVFFFP FLANGHILPT IDMAKLFSSR GVKATLITTH NNSAIFLKAI NRSKILGFDI
SVLTIKFPSA EFGLPEGYET ADQARSIDMM DEFFRACILL QEPLEELLKE HRPQALVADL
FFYWANDAAA KFGIPRLLFH GSSSFAMIAA ESVRRNKPYK NLSSDSDPFV VPDIPDKIIL
TKSQVPTPDE TEENNTHITE MWKNISESEN DCYGVIVNSF YELEPDYVDY CKNVLGRRAW
HIGPLSLCNN EGEDVAERGK KSDIDAHECL NWLDSKNPDS VVYVCFGSMA NFNAAQLHEL
AMGLEESGQE FIWVVRTCVD EEDESKWFPD GFEKRVQENN KGLIIKGWAP QVLILEHEAV
GAFVSHCGWN STLEGICGGV AMVTWPLFAE QFYNEKLMTD ILRTGVSVGS LQWSRVTTSA
VVVKRESISK AVRRLMAEEE GVDIRNRAKA LKEKAKKAVE GGGSSYSDLS ALLVELSSYP
HN