CGT_FRAAN
ID CGT_FRAAN Reviewed; 555 AA.
AC Q66PF4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Cinnamate beta-D-glucosyltransferase {ECO:0000303|PubMed:16443693, ECO:0000303|PubMed:17323078};
DE EC=2.4.1.177 {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
DE AltName: Full=UDP-glucose:cinnamate glucosyltransferase {ECO:0000303|PubMed:16443693};
DE Short=FaGT2 {ECO:0000303|PubMed:16443693};
GN Name=GT2 {ECO:0000312|EMBL:AAU09443.1};
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU09443.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=cv. Elsanta {ECO:0000269|PubMed:16443693};
RX PubMed=16443693; DOI=10.1104/pp.105.074955;
RA Lunkenbein S., Bellido M., Aharoni A., Salentijn E.M., Kaldenhoff R.,
RA Coiner H.A., Munoz-Blanco J., Schwab W.;
RT "Cinnamate metabolism in ripening fruit. Characterization of a UDP-
RT glucose:cinnamate glucosyltransferase from strawberry.";
RL Plant Physiol. 140:1047-1058(2006).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17323078; DOI=10.1007/s00425-007-0492-4;
RA Landmann C., Fink B., Schwab W.;
RT "FaGT2: a multifunctional enzyme from strawberry (Fragaria x ananassa)
RT fruits involved in the metabolism of natural and xenobiotic compounds.";
RL Planta 226:417-428(2007).
CC -!- FUNCTION: Broad spectrum multifunctional glucosyltransferase. Catalyzes
CC the formation of cinnamic acid and p-coumaric acid glucose esters
CC during fruit ripening. Accepted substrates range from derivatives of
CC cinnamic acid and benzoic acid to heterocyclic and aliphatic compounds,
CC resulting in the formation of O- and S-glucose esters and O-glucosides.
CC May also be involved in detoxification of xenobiotics.
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + UDP-alpha-D-glucose = 1-O-(trans-cinnamoyl)-
CC beta-D-glucose + UDP; Xref=Rhea:RHEA:13437, ChEBI:CHEBI:15669,
CC ChEBI:CHEBI:16279, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.177; Evidence={ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=356.9 uM for cinnamic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=730.0 uM for cinnamic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=80.8 uM for UDP-glucose {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=603.5 uM for p-coumaric acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=707.7 uM for caffeic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=358.5 uM for ferulic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=315.7 uM for 5-hydroxyferulic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=300.2 uM for sinapic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=502.6 uM for benzoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=464.4 uM for 3-hydroxybenzoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=642.4 uM for p-hydroxybenzoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=515.3 uM for vanillic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=108.0 uM for 3,4-dimethoxycinnamic acid
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC KM=411.2 uM for phenylpropionic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=431.0 uM for phenylbutyric acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=488.2 uM for 3-aminobenzoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=437.1 uM for 4-aminobenzoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=1.14 mM for 2,4,5-trichlorophenol {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=1.33 mM for trans-3-(2-furyl)acrylic acid
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC KM=3.23 mM for sorbic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=0.58 mM for 4-chlorocinnamic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=2.85 mM for 3,5-dichloro-4-hydroxybenzoic acid
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC KM=0.93 mM for trans-3-(3-pyridyl)acrylic acid
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC KM=2.74 mM for anthranilic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=5.76 mM for trans-2-hexenoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=2.75 mM for nicotinic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC KM=8.37 mM for thiobenzoic acid {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC Vmax=2.34 nmol/sec/mg enzyme with cinnamic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=6.43 nmol/sec/mg enzyme with cinnamic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=4.88 nmol/sec/mg enzyme with UDP-glucose as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=2.69 nmol/sec/mg enzyme with p-coumaric acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=2.59 nmol/sec/mg enzyme with caffeic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.65 nmol/sec/mg enzyme with ferulic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=2.24 nmol/sec/mg enzyme with 5-hydroxyferulic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.21 nmol/sec/mg enzyme with sinapic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.08 nmol/sec/mg enzyme with benzoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.05 nmol/sec/mg enzyme with 3-hydroxybenzoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=0.77 nmol/sec/mg enzyme with p-hydroxybenzoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.69 nmol/sec/mg enzyme with vanillic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=0.68 nmol/sec/mg enzyme with 3,4-dimethoxycinnamic acid as
CC substrate {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=0.17 nmol/sec/mg enzyme with phenylpropionic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=0.22 nmol/sec/mg enzyme with phenylbutyric acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=0.75 nmol/sec/mg enzyme with 3-aminobenzoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.73 nmol/sec/mg enzyme with 4-aminobenzoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=26.32 nmol/sec/mg enzyme with 2,4,5-trichlorophenol as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=12.96 nmol/sec/mg enzyme with trans-3-(2-furyl)acrylic acid as
CC substrate {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=18.20 nmol/sec/mg enzyme with sorbic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=3.23 nmol/sec/mg enzyme with 4-chlorocinnamic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=10.44 nmol/sec/mg enzyme with 3,5-dichloro-4-hydroxybenzoic acid
CC as substrate {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC Vmax=0.63 nmol/sec/mg enzyme with trans-3-(3-pyridyl)acrylic acid as
CC substrate {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=1.46 nmol/sec/mg enzyme with anthranilic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=2.36 nmol/sec/mg enzyme with trans-2-hexenoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=0.78 nmol/sec/mg enzyme with nicotinic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Vmax=2.04 nmol/sec/mg enzyme with thiobenzoic acid as substrate
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC Note=The kinetic constants are determined for the recombinant His(6)-
CC tagged protein. {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:16443693,
CC ECO:0000269|PubMed:17323078};
CC Temperature dependence:
CC Optimum temperature is 21 degrees Celsius.
CC {ECO:0000269|PubMed:16443693, ECO:0000269|PubMed:17323078};
CC -!- TISSUE SPECIFICITY: Highest expression detected in fruit, with lower
CC levels detected in flower and petiole. Barely detectable in leaf and
CC root. {ECO:0000269|PubMed:16443693}.
CC -!- DEVELOPMENTAL STAGE: Expression increases strongly along the fruit-
CC ripening stages, with maximal expression observed in fully ripe red
CC fruit. {ECO:0000269|PubMed:16443693}.
CC -!- INDUCTION: By oxidative stress and hydroxycinnamic acids. Down-
CC regulated by synthetic auxin naphthaleneacetic acid (NAA).
CC {ECO:0000269|PubMed:16443693}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000255}.
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DR EMBL; AY663785; AAU09443.1; -; mRNA.
DR AlphaFoldDB; Q66PF4; -.
DR SMR; Q66PF4; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR BioCyc; MetaCyc:MON-14069; -.
DR BRENDA; 2.4.1.177; 2320.
DR GO; GO:0050412; F:cinnamate beta-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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 Detoxification; Glycosyltransferase; Transferase.
FT CHAIN 1..555
FT /note="Cinnamate beta-D-glucosyltransferase"
FT /id="PRO_0000411993"
SQ SEQUENCE 555 AA; 61389 MW; 7CA53BF7482A7EC0 CRC64;
MGSESLVHVF LVSFIGQGHV NPLLRLGKRL AAKGLLVTFC TAECVGKEMR KSNGITDEPK
PVGDGFIRFE FFKDRWAEDE PMRQDLDLYL PQLELVGKEV IPEMIKKNAE QGRPVSCLIN
NPFIPWVCDV AESLGLPSAM LWVQSAACLA AYYHYYHGLV PFPSESDMFC DVQIPSMPLL
KYDEVPSFLY PTSPYPFLRR AILGQYGNLE KPFCILMDTF QELESEIIEY MARLCPIKAV
GPLFKNPKAQ NAVRGDFMEA DDSIIGWLDT KPKSSVVYIS FGSVVYLKQE QVDEIAHGLL
SSGVSFIWVM KPPHPDSGFE LLVLPEGFLE KAGDRGKVVQ WSPQEKILEH PSTACFVTHC
GWNSTMESLT SGMPVVAFPQ WGDQVTDAKY LVDEFKVGVR MCRGEAEDRV IPRDEVEKCL
LEATSGSKAA EMKQNALKWK AAAEAAFSEG GSSDRNLQAF VDEVRRISAS LNSKSSAVGY
VKSKINGVVE YVDSKLNGKA APVEEANTRT NGIAKVEQPK AANGKVEIAE LTPINGKVEI
AELKPINGKV ELVES
