ID   UGTA1_STABO             Reviewed;         463 AA.
AC   E7CQW6;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=UDP-glucosyltransferase A1 {ECO:0000303|PubMed:21073653};
DE            Short=GTI {ECO:0000303|PubMed:26298016};
DE            EC=2.4.1.- {ECO:0000269|PubMed:24242247};
GN   Name=ugtA1 {ECO:0000303|PubMed:21073653};
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=21073653; DOI=10.1111/j.1567-1364.2010.00695.x;
RA   Saerens K.M., Roelants S.L., Van Bogaert I.N., Soetaert W.;
RT   "Identification of the UDP-glucosyltransferase gene UGTA1, responsible for
RT   the first glucosylation step in the sophorolipid biosynthetic pathway of
RT   Candida bombicola ATCC 22214.";
RL   FEMS Yeast Res. 11:123-132(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, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=24242247; DOI=10.1128/aem.02886-13;
RA   Huang F.C., Peter A., Schwab W.;
RT   "Expression and characterization of CYP52 genes involved in the
RT   biosynthesis of sophorolipid and alkane metabolism from Starmerella
RT   bombicola.";
RL   Appl. Environ. Microbiol. 80:766-776(2014).
RN   [5]
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 first glycosylation step of sophorolipid
CC       biosynthesis, the coupling of glucose to a hydroxylated fatty acid to
CC       give rise to a glucolipid (PubMed:21073653, PubMed:23516968). Can
CC       glycosylate all hydroxyl fatty acids generated by cytochrome P450
CC       monooxygenases CYP52M1, CYP52N1 and CYP52E3 into their corresponding
CC       glucolipids. Main products are 17-O- and 18-O-(beta-D-glucopyranosyl)-
CC       octadecenoic acids (PubMed:24242247, PubMed:26298016).
CC       {ECO:0000269|PubMed:21073653, ECO:0000269|PubMed:23516968,
CC       ECO:0000269|PubMed:24242247, ECO:0000269|PubMed:26298016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=18-hydroxy-(9Z)-octadecenoate + UDP-alpha-D-glucose = (9Z)-18-
CC         hydroxyoctadec-9-enoate 18-O-beta-D-glucoside + H(+) + UDP;
CC         Xref=Rhea:RHEA:60960, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:78424, ChEBI:CHEBI:144061;
CC         Evidence={ECO:0000269|PubMed:26298016};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17-hydroxy-(9Z)-octadecenoate + UDP-alpha-D-glucose = (9Z)-17-
CC         hydroxyoctadec-9-enoate 17-O-beta-D-glucoside + H(+) + UDP;
CC         Xref=Rhea:RHEA:60956, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:144040, ChEBI:CHEBI:144057;
CC         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; HM440973; ADT71702.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7CQW6; -.
DR   SMR; E7CQW6; -.
DR   BioCyc; MetaCyc:MON-17750; -.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..463
FT                   /note="UDP-glucosyltransferase A1"
FT                   /id="PRO_0000443097"
SQ   SEQUENCE   463 AA;  50467 MW;  40A67D8FA704210D CRC64;
     MSPSSHKPLI LACGLPLSGH IMPVLSLVHG LTDDGYEATV VTGRAFEQKV RDVGADFVPL
     EGNADFDDHT LDDLVPGRKD MAPSFDRTVQ DVEHMMVATL PEQFAAIQRA FKKLSASGRP
     VVLVSEVLFF GAHPISLGAP GFKPAGWICL GVLPLLIRSD HTLGLDNDRS PEAHAKKLAM
     NHALEHQIFV KATAKHKEIC RELGCTEDPK FIWEHSYIAA DKFLQLCPPS LEFSRDHLPS
     NFKFAGSTPK HRTQFTPPSW WGDVLSAKRV IMVTQGTFAV SYKHLIVPTL EALKDEPDTL
     TVAILGRRGA KLPDDVVVPE NARVIDYFNY DALLPHVDAL VYNGGYGGLQ HSLSHSVPVV
     IAGDSEDKPM VASRAEAAGV AIDLKTGLPT VEQIKEAVDS IIGNPKFHEA SKKVQMELES
     HNSLKILEES IEEIASHDFG LLTKSDEETE DIPVKGPALA VSS