I7GT1_SOYBN
ID I7GT1_SOYBN Reviewed; 474 AA.
AC A6BM07;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Isoflavone 7-O-glucosyltransferase 1;
DE EC=2.4.1.170;
DE AltName: Full=UDP-glucose:isoflavone 7-O-glucosyltransferase;
DE Flags: Precursor;
GN Name=GmIF7GT1; Synonyms=GmIF7GT, UGT88E3; OrderedLocusNames=Glyma16g29400;
GN ORFNames=Gma.32181;
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], PROTEIN SEQUENCE OF 50-63; 121-133; 406-429 AND
RP 470-472, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF HIS-15; ASP-125; HIS-359; HIS-368; GLU-376;
RP GLU-392 AND GLU-456.
RX PubMed=17565994; DOI=10.1074/jbc.m702651200;
RA Noguchi A., Saito A., Homma Y., Nakao M., Sasaki N., Nishino T.,
RA Takahashi S., Nakayama T.;
RT "A UDP-glucose:isoflavone 7-O-glucosyltransferase from the roots of soybean
RT (glycine max) seedlings. Purification, gene cloning, phylogenetics, and an
RT implication for an alternative strategy of enzyme catalysis.";
RL J. Biol. Chem. 282:23581-23590(2007).
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 TISSUE SPECIFICITY.
RX PubMed=21741851; DOI=10.1016/j.plaphy.2011.06.007;
RA Livingstone J.M., Zolotarov Y., Stroemvik M.V.;
RT "Transcripts of soybean isoflavone 7-O-glucosyltransferase and
RT hydroxyisoflavanone dehydratase gene homologues are at least as abundant as
RT transcripts of their well known counterparts.";
RL Plant Physiol. Biochem. 49:1071-1075(2011).
CC -!- FUNCTION: Involved in the biosynthesis of isoflavonoids. Specific for
CC UDP-glucose. Can use genistein > daidzein > formononetin > quercetin >
CC kaempferol > 4,2',4',6'-tetrahydroxychalcone > apigenin > aureusidin >
CC esculetin > naringenin as substrates, but not cyanidin, trans-p-
CC coumaric acid, caffeic acid, benzoic acid, m- and p-hydroxybenzoic
CC acids, salicylic acid, salicyl alcohol, and hydroquinone.
CC {ECO:0000269|PubMed:17565994}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 7-hydroxyisoflavone + UDP-alpha-D-glucose = a 7-
CC hydroxyisoflavone 7-O-beta-D-glucoside + H(+) + UDP;
CC Xref=Rhea:RHEA:56344, ChEBI:CHEBI:15378, ChEBI:CHEBI:55465,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140301;
CC EC=2.4.1.170; Evidence={ECO:0000269|PubMed:17565994};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for genistein {ECO:0000269|PubMed:17565994};
CC KM=190 uM for UDP-glucose {ECO:0000269|PubMed:17565994};
CC Note=kcat is 0.74 sec(-1)for genistein (at pH 8.5 and 30 degrees
CC Celsius).;
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:17565994};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:17565994};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17565994}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots, leaves, cotyledons, epicotyls,
CC hypocotyls, roots, pods, seeds and flowers.
CC {ECO:0000269|PubMed:21741851}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB292164; BAF64416.1; -; mRNA.
DR RefSeq; NP_001235161.1; NM_001248232.1.
DR AlphaFoldDB; A6BM07; -.
DR SMR; A6BM07; -.
DR STRING; 3847.GLYMA16G29400.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; A6BM07; -.
DR EnsemblPlants; KRH08805; KRH08805; GLYMA_16G175600.
DR GeneID; 100101902; -.
DR Gramene; KRH08805; KRH08805; GLYMA_16G175600.
DR KEGG; gmx:100101902; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_3_2_1; -.
DR InParanoid; A6BM07; -.
DR OMA; GATEHEC; -.
DR OrthoDB; 508327at2759; -.
DR BRENDA; 2.4.1.170; 2483.
DR SABIO-RK; A6BM07; -.
DR Proteomes; UP000008827; Chromosome 16.
DR GO; GO:0050004; F:isoflavone 7-O-glucosyltransferase activity; IDA:UniProtKB.
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 Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW Transferase.
FT PROPEP 1..49
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:17565994"
FT /id="PRO_0000418446"
FT CHAIN 50..474
FT /note="Isoflavone 7-O-glucosyltransferase 1"
FT /id="PRO_0000418447"
FT MUTAGEN 15
FT /note="H->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 125
FT /note="D->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 359
FT /note="H->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 368
FT /note="H->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 376
FT /note="E->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 392
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 392
FT /note="E->D: Increased catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
FT MUTAGEN 456
FT /note="E->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:17565994"
SQ SEQUENCE 474 AA; 52036 MW; EC5C7AC14868AEE4 CRC64;
MKDTIVLYPN LGRGHLVSMV ELGKLILTHH PSLSITILIL TPPTTPSTTT TTLACDSNAQ
YIATVTATTP SITFHRVPLA ALPFNTPFLP PHLLSLELTR HSTQNIAVAL QTLAKASNLK
AIVIDFMNFN DPKALTENLN NNVPTYFYYT SGASTLALLL YYPTIHPTLI EKKDTDQPLQ
IQIPGLSTIT ADDFPNECKD PLSYACQVFL QIAETMMGGA GIIVNTFEAI EEEAIRALSE
DATVPPPLFC VGPVISAPYG EEDKGCLSWL NLQPSQSVVL LCFGSMGRFS RAQLKEIAIG
LEKSEQRFLW VVRTELGGAD DSAEELSLDE LLPEGFLERT KEKGMVVRDW APQAAILSHD
SVGGFVTHCG WNSVLEAVCE GVPMVAWPLY AEQKMNRMVM VKEMKVALAV NENKDGFVSS
TELGDRVREL MESDKGKEIR QRIFKMKMSA AEAMAEGGTS RASLDKLAKL WKQS
