708D1_SOYBN
ID 708D1_SOYBN Reviewed; 480 AA.
AC I1L3T1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=UDP-glycosyltransferase 708D1 {ECO:0000303|PubMed:25979175};
DE EC=2.4.1.360 {ECO:0000269|PubMed:25979175};
DE AltName: Full=UDP-glucose:2-hydroxyflavanone C-glucosyltransferase {ECO:0000305};
GN Name=UGT708D1 {ECO:0000303|PubMed:25979175};
GN OrderedLocusNames=Glyma09g29160;
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, 3D-STRUCTURE
RP MODELING, AND MUTAGENESIS OF HIS-20; ASP-85; ARG-202 AND ARG-292.
RX PubMed=25979175; DOI=10.1016/j.febslet.2015.05.010;
RA Hirade Y., Kotoku N., Terasaka K., Saijo-Hamano Y., Fukumoto A.,
RA Mizukami H.;
RT "Identification and functional analysis of 2-hydroxyflavanone C-
RT glucosyltransferase in soybean (Glycine max).";
RL FEBS Lett. 589:1778-1786(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18927222; DOI=10.1093/dnares/dsn024;
RA Umezawa T., Sakurai T., Totoki Y., Toyoda A., Seki M., Ishiwata A.,
RA Akiyama K., Kurotani A., Yoshida T., Mochida K., Kasuga M., Todaka D.,
RA Maruyama K., Nakashima K., Enju A., Mizukado S., Ahmed S., Yoshiwara K.,
RA Harada K., Tsubokura Y., Hayashi M., Sato S., Anai T., Ishimoto M.,
RA Funatsuki H., Teraishi M., Osaki M., Shinano T., Akashi R., Sakaki Y.,
RA Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Sequencing and analysis of approximately 40,000 soybean cDNA clones from a
RT full-length-enriched cDNA library.";
RL DNA Res. 15:333-346(2008).
CC -!- FUNCTION: UDP-glucose-dependent glucosyltransferase catalyzing the c-
CC glucosylation of the A ring of 2-hydroxynaringenin. Also active toward
CC phloretin, but not toward naringenin and apigenin.
CC {ECO:0000269|PubMed:25979175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-hydro-2'-hydroxy-beta-oxodihydrochalcone + UDP-alpha-D-
CC glucose = a 3'-(beta-D-glucopyranosyl)-2'-hydroxy-beta-
CC oxodihydrochalcone + H(+) + UDP; Xref=Rhea:RHEA:51504,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:142482, ChEBI:CHEBI:142483; EC=2.4.1.360;
CC Evidence={ECO:0000269|PubMed:25979175};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51505;
CC Evidence={ECO:0000269|PubMed:25979175};
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC003312; BAR73279.1; -; mRNA.
DR EMBL; CM000842; KRH38854.1; -; Genomic_DNA.
DR RefSeq; XP_003534077.1; XM_003534029.3.
DR AlphaFoldDB; I1L3T1; -.
DR SMR; I1L3T1; -.
DR STRING; 3847.GLYMA09G29160.1; -.
DR PRIDE; I1L3T1; -.
DR EnsemblPlants; KRH38854; KRH38854; GLYMA_09G162400.
DR Gramene; KRH38854; KRH38854; GLYMA_09G162400.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_1_1; -.
DR InParanoid; I1L3T1; -.
DR OMA; WEGEEGM; -.
DR OrthoDB; 508327at2759; -.
DR BRENDA; 2.4.1.360; 2483.
DR Proteomes; UP000008827; Chromosome 9.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
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 Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..480
FT /note="UDP-glycosyltransferase 708D1"
FT /id="PRO_0000435365"
FT REGION 291..292
FT /note="UDP"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT ACT_SITE 118
FT /note="Charge relay"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 19..22
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 141
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 353..356
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 371..379
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT BINDING 395..396
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:A0A0A1HA03"
FT MUTAGEN 20
FT /note="H->A: Loss of C-glucosyltransferase activity, but
FT acquisition of O-glucosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:25979175"
FT MUTAGEN 85
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:25979175"
FT MUTAGEN 202
FT /note="R->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:25979175"
FT MUTAGEN 292
FT /note="R->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:25979175"
SQ SEQUENCE 480 AA; 52515 MW; 1B30238A38231D08 CRC64;
MSSSEGVVHV AFLPSAGMGH LNPFLRLAAT FIRYGCKVTL ITPKPTVSLA ESNLISRFCS
SFPHQVTQLD LNLVSVDPTT VDTIDPFFLQ FETIRRSLHL LPPILSLLST PLSAFIYDIT
LITPLLSVIE KLSCPSYLYF TSSARMFSFF ARVSVLSASN PGQTPSSFIG DDGVKIPGFT
SPIPRSSVPP AILQASSNLF QRIMLEDSAN VTKLNNGVFI NSFEELEGEA LAALNGGKVL
EGLPPVYGVG PLMACEYEKG DEEGQKGCMS SIVKWLDEQS KGSVVYVSLG NRTETRREQI
KDMALGLIEC GYGFLWVVKL KRVDKEDEEG LEEVLGSELS SKVKEKGVVV KEFVDQVEIL
GHPSVGGFLS HGGWNSVTET VWKGVPCLSW PQHSDQKMSA EVIRMSGMGI WPEEWGWGTQ
DVVKGDEIAK RIKEMMSNES LRVKAGELKE AALKAAGVGG SCEVTIKRQI EEWKRNAQAN
