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U84B1_ARATH
ID   U84B1_ARATH             Reviewed;         456 AA.
AC   O22182;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=UDP-glycosyltransferase 84B1;
DE            EC=2.4.1.-;
GN   Name=UGT84B1; OrderedLocusNames=At2g23260; ORFNames=T20D16.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=11042215; DOI=10.1074/jbc.m007447200;
RA   Li Y., Baldauf S., Lim E.K., Bowles D.J.;
RT   "Phylogenetic analysis of the UDP-glycosyltransferase multigene family of
RT   Arabidopsis thaliana.";
RL   J. Biol. Chem. 276:4338-4343(2001).
RN   [6]
RP   FUNCTION.
RX   PubMed=15352060; DOI=10.1002/bit.20154;
RA   Lim E.K., Ashford D.A., Hou B., Jackson R.G., Bowles D.J.;
RT   "Arabidopsis glycosyltransferases as biocatalysts in fermentation for
RT   regioselective synthesis of diverse quercetin glucosides.";
RL   Biotechnol. Bioeng. 87:623-631(2004).
CC   -!- FUNCTION: Possesses low quercetin 7-O-glucosyltransferase activity in
CC       vitro. {ECO:0000269|PubMed:15352060}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AC002391; AAB87119.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07435.1; -; Genomic_DNA.
DR   EMBL; AK118431; BAC43040.1; -; mRNA.
DR   EMBL; BT005368; AAO63432.1; -; mRNA.
DR   PIR; T00506; T00506.
DR   RefSeq; NP_179907.1; NM_127890.3.
DR   AlphaFoldDB; O22182; -.
DR   SMR; O22182; -.
DR   STRING; 3702.AT2G23260.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; O22182; -.
DR   PRIDE; O22182; -.
DR   ProteomicsDB; 242811; -.
DR   EnsemblPlants; AT2G23260.1; AT2G23260.1; AT2G23260.
DR   GeneID; 816858; -.
DR   Gramene; AT2G23260.1; AT2G23260.1; AT2G23260.
DR   KEGG; ath:AT2G23260; -.
DR   Araport; AT2G23260; -.
DR   TAIR; locus:2058563; AT2G23260.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_1_1; -.
DR   InParanoid; O22182; -.
DR   OMA; WIPEDSC; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; O22182; -.
DR   BioCyc; ARA:AT2G23260-MON; -.
DR   BioCyc; MetaCyc:AT2G23260-MON; -.
DR   SABIO-RK; O22182; -.
DR   PRO; PR:O22182; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22182; baseline and differential.
DR   Genevisible; O22182; AT.
DR   GO; GO:0047215; F:indole-3-acetate beta-glucosyltransferase activity; IDA:TAIR.
DR   GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IDA:TAIR.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR   GO; GO:0090354; P:regulation of auxin metabolic process; IMP:TAIR.
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   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..456
FT                   /note="UDP-glycosyltransferase 84B1"
FT                   /id="PRO_0000409124"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         332..334
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..357
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         371..374
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  50714 MW;  6770DA38A7709602 CRC64;
     MGSSEGQETH VLMVTLPFQG HINPMLKLAK HLSLSSKNLH INLATIESAR DLLSTVEKPR
     YPVDLVFFSD GLPKEDPKAP ETLLKSLNKV GAMNLSKIIE EKRYSCIISS PFTPWVPAVA
     ASHNISCAIL WIQACGAYSV YYRYYMKTNS FPDLEDLNQT VELPALPLLE VRDLPSFMLP
     SGGAHFYNLM AEFADCLRYV KWVLVNSFYE LESEIIESMA DLKPVIPIGP LVSPFLLGDG
     EEETLDGKNL DFCKSDDCCM EWLDKQARSS VVYISFGSML ETLENQVETI AKALKNRGLP
     FLWVIRPKEK AQNVAVLQEM VKEGQGVVLE WSPQEKILSH EAISCFVTHC GWNSTMETVV
     AGVPVVAYPS WTDQPIDARL LVDVFGIGVR MRNDSVDGEL KVEEVERCIE AVTEGPAAVD
     IRRRAAELKR VARLALAPGG SSTRNLDLFI SDITIA
 
 
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