NDPGT_BACLD
ID NDPGT_BACLD Reviewed; 396 AA.
AC Q65JC2; Q62UT0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=NDP-glycosyltransferase YjiC {ECO:0000305};
DE EC=2.4.1.384 {ECO:0000269|PubMed:23542617, ECO:0000269|PubMed:23974133, ECO:0000269|PubMed:24170092, ECO:0000269|PubMed:24893262, ECO:0000269|PubMed:24949266, ECO:0000269|PubMed:25239890, ECO:0000269|PubMed:27444326};
DE AltName: Full=UDP-glucosyltransferase YjiC {ECO:0000303|PubMed:23542617};
GN Name=yjiC {ECO:0000312|EMBL:AAU23479.1};
GN OrderedLocusNames=BL00446 {ECO:0000312|EMBL:AAU23479.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=23542617; DOI=10.1128/aem.00409-13;
RA Pandey R.P., Li T.F., Kim E.H., Yamaguchi T., Park Y.I., Kim J.S.,
RA Sohng J.K.;
RT "Enzymatic synthesis of novel phloretin glucosides.";
RL Appl. Environ. Microbiol. 79:3516-3521(2013).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=23974133; DOI=10.1128/aem.02057-13;
RA Pandey R.P., Parajuli P., Koirala N., Park J.W., Sohng J.K.;
RT "Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by
RT YjiC.";
RL Appl. Environ. Microbiol. 79:6833-6838(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=24170092; DOI=10.1007/s10059-013-0164-0;
RA Gurung R.B., Kim E.H., Oh T.J., Sohng J.K.;
RT "Enzymatic synthesis of apigenin glucosides by glucosyltransferase (YjiC)
RT from Bacillus licheniformis DSM 13.";
RL Mol. Cells 36:355-361(2013).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=24893262; DOI=10.1016/j.carres.2014.03.011;
RA Pandey R.P., Gurung R.B., Parajuli P., Koirala N., Tuoi L.T., Sohng J.K.;
RT "Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation
RT toward flavonoids.";
RL Carbohydr. Res. 393:26-31(2014).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=25239890; DOI=10.1128/aem.02076-14;
RA Pandey R.P., Parajuli P., Shin J.Y., Lee J., Lee S., Hong Y.S., Park Y.I.,
RA Kim J.S., Sohng J.K.;
RT "Enzymatic biosynthesis of novel resveratrol glucoside and glycoside
RT derivatives.";
RL Appl. Environ. Microbiol. 80:7235-7243(2014).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=24949266; DOI=10.1186/s13568-014-0031-1;
RA Parajuli P., Pandey R.P., Koirala N., Yoon Y.J., Kim B.G., Sohng J.K.;
RT "Enzymatic synthesis of epothilone A glycosides.";
RL AMB Express 4:31-31(2014).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=27444326; DOI=10.1016/j.enzmictec.2016.05.006;
RA Pandey R.P., Parajuli P., Gurung R.B., Sohng J.K.;
RT "Donor specificity of YjiC glycosyltransferase determines the conjugation
RT of cytosolic NDP-sugar in in vivo glycosylation reactions.";
RL Enzyme Microb. Technol. 91:26-33(2016).
RN [9]
RP FUNCTION IN N- AND S-GLYCOSYLATION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=32238768; DOI=10.4014/jmb.2001.01024;
RA Bashyal P., Thapa S.B., Kim T.S., Pandey R.P., Sohng J.K.;
RT "Exploring the nucleophilic N- and S-glycosylation capacity of Bacillus
RT licheniformis YjiC enzyme.";
RL J. Microbiol. Biotechnol. 30:1092-1096(2020).
CC -!- FUNCTION: Glycosyltransferase that can glycosylate a wide range of
CC substrates, including various flavonoids (flavones, flavonols,
CC flavanones, flavanols, chalcones), isoflavonoids and stilbenes, to
CC produce multiple glycosylated products (PubMed:23542617,
CC PubMed:23974133, PubMed:24170092, PubMed:24893262, PubMed:25239890,
CC PubMed:24949266, PubMed:27444326, PubMed:32238768). It can accept
CC diverse nucleotide diphosphate-D/L-sugars as donors, including ADP-,
CC GDP-, CDP-, TDP- or UDP-alpha-D-glucose, and catalyzes O-, N-, or S-
CC glycosylation (PubMed:23542617, PubMed:23974133, PubMed:24170092,
CC PubMed:24893262, PubMed:25239890, PubMed:24949266, PubMed:27444326,
CC PubMed:32238768). In vitro, catalyzes the glycosylation of, among
CC others, apigenin, 3-hydroxyflavone, phloretin or resveratrol, resulting
CC in multiple glucosylated products, along with mono-, di-, tri- and
CC tetraglucosides (PubMed:23542617, PubMed:23974133, PubMed:24170092,
CC PubMed:24893262, PubMed:25239890, PubMed:27444326). Can also catalyze
CC the glycosylation of the macrolide epothilone A with diverse NDP-D/L-
CC sugars, forming different epothilone A glycoside derivatives
CC (PubMed:24949266). {ECO:0000269|PubMed:23542617,
CC ECO:0000269|PubMed:23974133, ECO:0000269|PubMed:24170092,
CC ECO:0000269|PubMed:24893262, ECO:0000269|PubMed:24949266,
CC ECO:0000269|PubMed:25239890, ECO:0000269|PubMed:27444326,
CC ECO:0000269|PubMed:32238768}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-glycose + an acceptor = a glycosylated acceptor + NDP.;
CC EC=2.4.1.384; Evidence={ECO:0000269|PubMed:23542617,
CC ECO:0000269|PubMed:23974133, ECO:0000269|PubMed:24170092,
CC ECO:0000269|PubMed:24893262, ECO:0000269|PubMed:24949266,
CC ECO:0000269|PubMed:25239890, ECO:0000269|PubMed:27444326,
CC ECO:0000269|PubMed:32238768};
CC -!- BIOTECHNOLOGY: Such glycosyltransferases with substrate flexibility and
CC less regioselectivity can be utilized for glucosylation of a broad
CC range of pharmacologically and industrially important compounds
CC (PubMed:24170092). Glycosylation is an efficient tool for generating
CC biologically potent and diverse novel natural and unnatural product
CC glycoside compounds with enhanced drug efficacy. For instance,
CC generation of novel resveratrol glycosides could facilitate the
CC development of drugs to treat oxidative- stress-induced diseases and to
CC provide antiaging functions (PubMed:25239890). Glycosylation of
CC epothilones, a class of potential cancer drugs, may improve their
CC efficacy as therapeutic drugs (PubMed:24949266). YjiC is a promiscuous
CC enzyme for conjugating diverse sugars at amine and thiol functional
CC groups of small molecules applicable for generating glycofunctionalized
CC chemical diversity libraries (PubMed:32238768).
CC {ECO:0000269|PubMed:24170092, ECO:0000269|PubMed:24949266,
CC ECO:0000269|PubMed:25239890, ECO:0000269|PubMed:32238768}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CP000002; AAU23479.1; -; Genomic_DNA.
DR RefSeq; WP_003182014.1; NC_006322.1.
DR SMR; Q65JC2; -.
DR STRING; 279010.BL00446; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblBacteria; AAU23479; AAU23479; BL00446.
DR GeneID; 66216042; -.
DR KEGG; bli:BL00446; -.
DR PATRIC; fig|279010.13.peg.1950; -.
DR eggNOG; COG1819; Bacteria.
DR HOGENOM; CLU_000537_7_1_9; -.
DR OMA; NIPAYGH; -.
DR OrthoDB; 1485440at2; -.
DR BRENDA; 2.4.1.81; 669.
DR BRENDA; 2.4.1.B84; 669.
DR BRENDA; 2.4.1.B85; 669.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR006326; UDPGT_MGT-like.
DR Pfam; PF00201; UDPGT; 1.
DR TIGRFAMs; TIGR01426; MGT; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="NDP-glycosyltransferase YjiC"
FT /id="PRO_0000455005"
FT BINDING 18
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O34539"
FT BINDING 234
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O34539"
FT BINDING 283
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O34539"
FT BINDING 298
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O34539"
FT BINDING 302..306
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O34539"
SQ SEQUENCE 396 AA; 44659 MW; 8169E4D94CB276D7 CRC64;
MGHKHIAIFN IPAHGHINPT LALTASLVKR GYRVTYPVTD EFVKAVEETG AEPLNYRSTL
NIDPQQIREL MKNKKDMSQA PLMFIKEMEE VLPQLEALYE NDKPDLILFD FMAMAGKLLA
EKFGIEAVRL CSTYAQNEHF TFRSISEEFK IELTPEQEDA LKNSNLPSFN FEDMFEPAKL
NIVFMPRAFQ PYGETFDERF SFVGPSLAKR KFQEKETPII SDSGRPVMLI SLGTAFNAWP
EFYHMCIEAF RDTKWQVIMA VGTTIDPESF DDIPENFSIH QRVPQLEILK KAELFITHGG
MNSTMEGLNA GVPLVAVPQM PEQEITARRV EELGLGKHLQ PEDTTAASLR EAVSQTDGDP
HVLKRIQDMQ KHIKQAGGAE KAADEIEAFL APAGVK
