ID   UGT9_CATRO              Reviewed;         474 AA.
AC   W8JMV4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=UDP glycosyltransferase 9 {ECO:0000303|PubMed:24710322};
DE            Short=CrUGT9 {ECO:0000303|PubMed:24710322};
DE            EC=2.4.1.- {ECO:0000255|RuleBase:RU362057};
GN   Name=UGT9 {ECO:0000303|PubMed:24710322};
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Bright Eyes;
RX   PubMed=24710322; DOI=10.1038/ncomms4606;
RA   Miettinen K., Dong L., Navrot N., Schneider T., Burlat V., Pollier J.,
RA   Woittiez L., van der Krol S., Lugan R., Ilc T., Verpoorte R.,
RA   Oksman-Caldentey K.M., Martinoia E., Bouwmeester H., Goossens A.,
RA   Memelink J., Werck-Reichhart D.;
RT   "The seco-iridoid pathway from Catharanthus roseus.";
RL   Nat. Commun. 5:3606-3606(2014).
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KF302080; AHK60847.1; -; mRNA.
DR   AlphaFoldDB; W8JMV4; -.
DR   SMR; W8JMV4; -.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
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; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..474
FT                   /note="UDP glycosyltransferase 9"
FT                   /id="PRO_0000446419"
FT   BINDING         296
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         349..350
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         367..375
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
FT   BINDING         389..392
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M156"
SQ   SEQUENCE   474 AA;  53544 MW;  EA2F07F1478DD5B6 CRC64;
     MGTIDIITSP TPIHILAFPF PAKGHINPLL HLCNRLASKG FKITLITTVS TLKSVKTSKA
     NGIDIESIPD GIPQEQNHQI ITVMEMNMEL YFKQFKASAI ENTTKLIQKL KTKNPPPKVL
     IYDSSMPWIL EVAHEQGLLG ASFFTQPCSV SAIYYHMLQG TIKLPLENSE NGMVSLPYLP
     LLEKKDLPGV QQFEDNSEAL AELLADQFSN IDDVDYVLFN TFDALEIEVV NWMGSKWPIL
     TVGPTAPTSM FLLDKKQKNY EDGRSINYLF ETNTEVCMKW LDQREIDTVI YVSFGSLASL
     TEEQMEQVSQ ALIRSNCYFL WVVREEEENK LPKDFKETTS KKKGLVINWC PQLDVLAHKS
     VACFMTHCGW NSTLEALCSG VPMICMPQWA DQTTNAKLIE HVWKIGVGVN KSDENGIVKR
     EDIEDCIRQV IESERGKELK RNAIKWKELA KEAVSEGGSS YNNIQEFSSS LLFN