UGT79_ORYSJ
ID UGT79_ORYSJ Reviewed; 466 AA.
AC Q7XT97; A3AR29;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=UDP-glycosyltransferase 79 {ECO:0000305};
DE Short=OsUGT79 {ECO:0000303|PubMed:26197338};
DE EC=2.4.1.- {ECO:0000269|PubMed:26197338};
DE AltName: Full=Deoxynivalenol-UDP-glucosyltransferase {ECO:0000303|PubMed:27715009};
GN Name=UGT79 {ECO:0000303|PubMed:26197338};
GN Synonyms=OS79 {ECO:0000303|PubMed:27715009};
GN OrderedLocusNames=Os04g0206600 {ECO:0000312|EMBL:BAF14158.1},
GN LOC_Os04g12970 {ECO:0000305};
GN ORFNames=OsJ_13826 {ECO:0000312|EMBL:EAZ29768.1},
GN OSJNBa0052O21.15 {ECO:0000312|EMBL:CAE01609.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP INDUCTION BY GAMMA RAY.
RX PubMed=24631263; DOI=10.1016/j.gene.2014.02.060;
RA Hwang S.G., Kim D.S., Hwang J.E., Han A.R., Jang C.S.;
RT "Identification of rice genes associated with cosmic-ray response via co-
RT expression gene network analysis.";
RL Gene 541:82-91(2014).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26197338; DOI=10.3390/toxins7072685;
RA Michlmayr H., Malachova A., Varga E., Kleinova J., Lemmens M.,
RA Newmister S., Rayment I., Berthiller F., Adam G.;
RT "Biochemical characterization of a recombinant UDP-glucosyltransferase from
RT rice and enzymatic production of deoxynivalenol-3-O-beta-D-glucoside.";
RL Toxins 7:2685-2700(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE-DERIVED
RP DONOR, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-27;
RP ASP-120; THR-291 AND HIS-361.
RX PubMed=27715009; DOI=10.1021/acs.biochem.6b00709;
RA Wetterhorn K.M., Newmister S.A., Caniza R.K., Busman M., McCormick S.P.,
RA Berthiller F., Adam G., Rayment I.;
RT "Crystal Structure of Os79 (Os04g0206600) from Oryza sativa: A UDP-
RT glucosyltransferase Involved in the Detoxification of Deoxynivalenol.";
RL Biochemistry 55:6175-6186(2016).
CC -!- FUNCTION: Involved in the detoxification of the Fusarium mycotoxin
CC deoxynivalenol by the transfer of glucose from UDP-D-glucose to the
CC hydroxyl group at C-3, forming deoxynivalenol-3-O-beta-D-glucoside.
CC {ECO:0000269|PubMed:26197338, ECO:0000269|PubMed:27715009}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for deoxynivalenol {ECO:0000269|PubMed:26197338};
CC KM=61 uM for deoxynivalenol {ECO:0000269|PubMed:27715009};
CC KM=22 uM for HT-2 mycotoxin {ECO:0000269|PubMed:27715009};
CC KM=35 uM for nivalenol {ECO:0000269|PubMed:27715009};
CC KM=2.2 mM for UDP-D-glucose {ECO:0000269|PubMed:26197338};
CC Vmax=0.36 umol/min/mg enzyme with deoxynivalenol as substrate
CC {ECO:0000269|PubMed:26197338};
CC -!- INDUCTION: Induced by exposition to gamma ray.
CC {ECO:0000269|PubMed:24631263}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AL606590; CAE01609.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14158.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS88104.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ29768.1; -; Genomic_DNA.
DR EMBL; AK106302; BAG97673.1; -; mRNA.
DR RefSeq; XP_015635481.1; XM_015779995.1.
DR PDB; 5TMB; X-ray; 2.34 A; A=1-466.
DR PDB; 5TMD; X-ray; 2.19 A; A=1-466.
DR PDB; 5TME; X-ray; 1.78 A; A=1-466.
DR PDB; 6BK0; X-ray; 1.47 A; A=1-466.
DR PDB; 6BK1; X-ray; 1.58 A; A=1-466.
DR PDB; 6BK2; X-ray; 1.68 A; A=1-466.
DR PDB; 6BK3; X-ray; 2.17 A; A=1-466.
DR PDBsum; 5TMB; -.
DR PDBsum; 5TMD; -.
DR PDBsum; 5TME; -.
DR PDBsum; 6BK0; -.
DR PDBsum; 6BK1; -.
DR PDBsum; 6BK2; -.
DR PDBsum; 6BK3; -.
DR AlphaFoldDB; Q7XT97; -.
DR SMR; Q7XT97; -.
DR STRING; 4530.OS04T0206600-01; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q7XT97; -.
DR PRIDE; Q7XT97; -.
DR EnsemblPlants; Os04t0206600-01; Os04t0206600-01; Os04g0206600.
DR GeneID; 4335166; -.
DR Gramene; Os04t0206600-01; Os04t0206600-01; Os04g0206600.
DR KEGG; osa:4335168; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_001724_0_1_1; -.
DR InParanoid; Q7XT97; -.
DR OMA; RNATRLM; -.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0098754; P:detoxification; 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 3D-structure; Detoxification; Glycosyltransferase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..466
FT /note="UDP-glycosyltransferase 79"
FT /id="PRO_0000441955"
FT BINDING 27
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:27715009,
FT ECO:0007744|PDB:5TMD"
FT BINDING 142
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:27715009,
FT ECO:0007744|PDB:5TMD"
FT BINDING 291
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:27715009,
FT ECO:0007744|PDB:5TMD"
FT BINDING 344
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:27715009,
FT ECO:0007744|PDB:5TMD"
FT BINDING 361..369
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:27715009,
FT ECO:0007744|PDB:5TMD"
FT BINDING 385..386
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:27715009,
FT ECO:0007744|PDB:5TMD"
FT MUTAGEN 27
FT /note="H->N: Loss of activity; when associated with A-120."
FT /evidence="ECO:0000269|PubMed:27715009"
FT MUTAGEN 120
FT /note="D->A: Loss of activity; when associated with N-27."
FT /evidence="ECO:0000269|PubMed:27715009"
FT MUTAGEN 291
FT /note="T->A,V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27715009"
FT MUTAGEN 361
FT /note="H->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:27715009"
FT CONFLICT 81
FT /note="A -> G (in Ref. 5; EAZ29768)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="P -> S (in Ref. 5; EAZ29768)"
FT /evidence="ECO:0000305"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 85..109
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6BK0"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:6BK0"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:6BK0"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6BK0"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6BK0"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:6BK0"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:6BK0"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 413..425
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 429..447
FT /evidence="ECO:0007829|PDB:6BK0"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:6BK0"
SQ SEQUENCE 466 AA; 51028 MW; 24B7F0C93B1BB504 CRC64;
MGSMSTPAAS ANGGQVLLLP FPAAQGHTNP MLQFGRRLAY HGLRPTLVTT RYVLSTTPPP
GDPFRVAAIS DGFDDASGMA ALPDPGEYLR TLEAHGARTL AELLLSEARA GRPARVLVYD
PHLPWARRVA RAAGVATAAF LSQPCAVDLI YGEVCARRLA LPVTPTDARG LYARGVLGVE
LGPDDVPPFV AAPELTPAFC EQSIEQFAGL EDDDDVLVNS FSDLEPKEAA YMESTWRAKT
IGPSLPSFYL DDGRLRSNTA YGFNLFRSTV PCMEWLDKQP PRSVVLVSYG TVSTFDVAKL
EELGNGLCNS GKPFLWVVRS NEEHKLSVQL RKKCEKRGLI VPFCPQLEVL AHKATGCFLS
HCGWNSTLEA IVNGVPLVAM PHWADQPTIS KYVESLWGMG VRVQLDKSGI LQREEVERCI
REVMDGDRKE DYRRNATRLM KKAKESMQEG GSSDKNIAEF AAKYSN
