ID   UGTB1_STABO             Reviewed;         432 AA.
AC   E9L011;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=UDP-glucosyltransferase B1 {ECO:0000303|PubMed:21456054};
DE            Short=GTII {ECO:0000303|PubMed:26298016};
DE            EC=2.4.1.- {ECO:0000269|PubMed:26298016};
GN   Name=ugtB1 {ECO:0000303|PubMed:21456054};
OS   Starmerella bombicola (Yeast) (Candida bombicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Starmerella.
OX   NCBI_TaxID=75736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX   PubMed=21456054; DOI=10.1002/yea.1838;
RA   Saerens K.M., Zhang J., Saey L., Van Bogaert I.N., Soetaert W.;
RT   "Cloning and functional characterization of the UDP-glucosyltransferase
RT   UgtB1 involved in sophorolipid production by Candida bombicola and creation
RT   of a glucolipid-producing yeast strain.";
RL   Yeast 28:279-292(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX   PubMed=23964782; DOI=10.1021/pr400392a;
RA   Ciesielska K., Li B., Groeneboer S., Van Bogaert I., Lin Y.C., Soetaert W.,
RA   Van de Peer Y., Devreese B.;
RT   "SILAC-based proteome analysis of Starmerella bombicola sophorolipid
RT   production.";
RL   J. Proteome Res. 12:4376-4392(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=23516968; DOI=10.1111/mmi.12200;
RA   Van Bogaert I.N., Holvoet K., Roelants S.L., Li B., Lin Y.C.,
RA   Van de Peer Y., Soetaert W.;
RT   "The biosynthetic gene cluster for sophorolipids: a biotechnological
RT   interesting biosurfactant produced by Starmerella bombicola.";
RL   Mol. Microbiol. 88:501-509(2013).
RN   [4]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=26298016; DOI=10.1093/femsyr/fov075;
RA   Saerens K.M., Van Bogaert I.N., Soetaert W.;
RT   "Characterization of sophorolipid biosynthetic enzymes from Starmerella
RT   bombicola.";
RL   FEMS Yeast Res. 15:0-0(2015).
CC   -!- FUNCTION: Catalyzes the second glycosylation step of sophorolipid
CC       biosynthesis, the further glucosylation of the previoulsy formed
CC       glucolipid to give rise to an acidic sophorolipid.
CC       {ECO:0000269|PubMed:21456054, ECO:0000269|PubMed:23516968,
CC       ECO:0000269|PubMed:26298016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-17-hydroxyoctadec-9-enoate 17-O-beta-D-glucoside + UDP-
CC         alpha-D-glucose = (9Z)-17-hydroxyoctadec-9-enoate 17-O-sophoroside +
CC         H(+) + UDP; Xref=Rhea:RHEA:60964, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:144057,
CC         ChEBI:CHEBI:144058; Evidence={ECO:0000269|PubMed:26298016};
CC   -!- INDUCTION: Induced in early stationary phase (at protein level).
CC       {ECO:0000269|PubMed:23964782}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; HM440974; ADT71703.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9L011; -.
DR   SMR; E9L011; -.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..432
FT                   /note="UDP-glucosyltransferase B1"
FT                   /id="PRO_0000443098"
SQ   SEQUENCE   432 AA;  46155 MW;  35F94A170D8E43C7 CRC64;
     MAIEKPVIVA CACPLAGHVG PVLSLVRGLL NRGYEVTFVT GNAFKEKVIE AGCTFVPLQG
     RADYHEYNLP EIAPGLLTIP PGLEQTGYSM NEIFVKAIPE QYDALQTALK QVEAENKSAV
     VIGETMFLGV HPISLGAPGL KPQGVITLGT IPCMLKAEKA PGVPSLEPMI DTLVRQQVFQ
     PGTDSEKEIM KTLGATKEPE FLLENIYSSP DRFLQLCPPS LEFHLTSPPP GFSFAGSAPH
     VKSAGLATPP HLPSWWPDVL SAKRLIVVTQ GTAAINYEDL LIPALQAFAD EEDTLVVGIL
     GVKGASLPDS VKVPANARIV DYFPYDELLP HASVFIYNGG YGGLQHSLSH GVPVIIGGGM
     LVDKPAVASR AVWAGVGYDL QTLQATSELV STAVKEVLAT PSYHEKAMAV KKELEKYKSL
     DILESAISEL AS