EMT1_PSEA3
ID EMT1_PSEA3 Reviewed; 617 AA.
AC M9MH90; D3KZ17;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Erythritol-mannosyl-transferase 1 {ECO:0000303|PubMed:23558529};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:A0A0D1DZV5};
DE AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein EMT1 {ECO:0000303|PubMed:31923270};
GN Name=EMT1 {ECO:0000303|PubMed:23558529}; ORFNames=PANT_19c00001;
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=T-34;
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-617, FUNCTION, DISRUPTION
RP PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=20564650; DOI=10.1002/yea.1794;
RA Morita T., Ito E., Kitamoto H.K., Takegawa K., Fukuoka T., Imura T.,
RA Kitamoto D.;
RT "Identification of the gene PaEMT1 for biosynthesis of mannosylerythritol
RT lipids in the basidiomycetous yeast Pseudozyma antarctica.";
RL Yeast 27:905-917(2010).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=16233292; DOI=10.1263/jbb.94.187;
RA Kitamoto D., Isoda H., Nakahara T.;
RT "Functions and potential applications of glycolipid biosurfactants--from
RT energy-saving materials to gene delivery carriers.";
RL J. Biosci. Bioeng. 94:187-201(2002).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=17428643; DOI=10.1016/j.colsurfb.2007.03.003;
RA Ito S., Imura T., Fukuoka T., Morita T., Sakai H., Abe M., Kitamoto D.;
RT "Kinetic studies on the interactions between glycolipid biosurfactant
RT assembled monolayers and various classes of immunoglobulins using surface
RT plasmon resonance.";
RL Colloids Surf. B Biointerfaces 58:165-171(2007).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=17279642; DOI=10.1021/la0620814;
RA Imura T., Hikosaka Y., Worakitkanchanakul W., Sakai H., Abe M., Konishi M.,
RA Minamikawa H., Kitamoto D.;
RT "Aqueous-phase behavior of natural glycolipid biosurfactant
RT mannosylerythritol lipid A: sponge, cubic, and lamellar phases.";
RL Langmuir 23:1659-1663(2007).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=19341364; DOI=10.1042/ba20090033;
RA Morita T., Fukuoka T., Imura T., Kitamoto D.;
RT "Production of glycolipid biosurfactants by basidiomycetous yeasts.";
RL Biotechnol. Appl. Biochem. 53:39-49(2009).
RN [7]
RP BIOTECHNOLOGY.
RX DOI=10.1016/j.cocis.2009.05.009;
RA Kitamoto D., Morita T., Fukuoka T., Konishi M., Imura T.;
RT "Self-assembling properties of glycolipid biosurfactants and their
RT potential applications.";
RL Curr. Opin. Colloid Interface Sci. 14:315-328(2009).
RN [8]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=31923270; DOI=10.1371/journal.pone.0227295;
RA Wada K., Koike H., Fujii T., Morita T.;
RT "Targeted transcriptomic study of the implication of central metabolic
RT pathways in mannosylerythritol lipids biosynthesis in Pseudozyma antarctica
RT T-34.";
RL PLoS ONE 15:E0227295-E0227295(2020).
CC -!- FUNCTION: Glycosyltransferase; part of the gene cluster that mediates
CC the biosynthesis of mannosylerythritol lipids (MELs), surface-active
CC substances that enhance the availability of water-insoluble substrates
CC (Probable) (PubMed:20564650, PubMed:31923270). Depending on the number
CC of acetyl groups, mannosylerythritol lipids can be differentiated into
CC MEL A (fully acetylated), MEL B and MEL C (monoacetylated at R-6 and R-
CC 4, respectively), and the fully deacetylated MEL D (By similarity). The
CC first step in the pathway is the generation of mannosylerythritol by
CC the glycosyltransferase EMT1 which catalyzes the transfer of GDP-
CC mannose to the C-4 atom of meso-erythritol (PubMed:20564650). This
CC reaction has to be stereospecific, since only mannosyl-D-erythritol is
CC generated (Probable). The produced disaccharide is subsequently
CC acylated with fatty acids of various lengths by the acyltransferases
CC MAC1 and MAC2 at positions C-2 and C-3, repectively (Probable). The
CC existence of MEL derivatives which carry an acetyl group at C-2 implies
CC that at least MAC1 also accepts acetyl-CoA as a donor (Probable). The
CC final step of MEL biosynthesis is the acetylation of the fully acylated
CC mannosylerythritol lipids catalyzed by the acetyl-CoA-dependent
CC acetyltransferase MAT1 (Probable). MAT1 displays a relaxed
CC regioselectivity and is able to transfer acetylgroups to both positions
CC C-4 and C-6 of the mannosyl moiety (Probable).
CC {ECO:0000250|UniProtKB:A0A0D1DZV5, ECO:0000269|PubMed:20564650,
CC ECO:0000269|PubMed:31923270, ECO:0000305|PubMed:23558529,
CC ECO:0000305|PubMed:31923270}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31923270}.
CC -!- INDUCTION: Expression is induced when cells are grown in cultures
CC containing vegetable oil as the carbon source.
CC {ECO:0000269|PubMed:31923270}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of mannosylerythritol
CC lipids (MELs) (PubMed:20564650). Leads to low-temperature sensitivity
CC and affect the cell morphology by impairing formation of filamentous
CC forms (PubMed:20564650). {ECO:0000269|PubMed:20564650}.
CC -!- BIOTECHNOLOGY: MELs not only have high potential as eco-friendly
CC biosurfactants due to their excellent surface activity, but also have
CC attracted considerable recent interest because of thei runique
CC properties, including self-assembly, anti-tumor and cell
CC differentiation induction activities, and moisturizing and hair-
CC repairing properties. {ECO:0000269|PubMed:16233292,
CC ECO:0000269|PubMed:17279642, ECO:0000269|PubMed:17428643,
CC ECO:0000269|PubMed:19341364, ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAI77915.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB548311; BAI77915.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DF196785; GAC75887.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MH90; -.
DR STRING; 1151754.M9MH90; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblFungi; GAC75887; GAC75887; PANT_19c00001.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..617
FT /note="Erythritol-mannosyl-transferase 1"
FT /id="PRO_0000449533"
FT REGION 365..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 142
FT /note="M -> V (in Ref. 2; BAI77915)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="N -> D (in Ref. 2; BAI77915)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="M -> I (in Ref. 2; BAI77915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 68768 MW; E539947CA292E0B3 CRC64;
MKIALLANPA RGEINVLLAT AYELIRLGHE VVFLTGSSFR NAIAEFKDEQ NDKLLASRIQ
FSDLGTAKAF EDFTRGMQSH LKGLRKPPGD YSSMEICQIV ALVTEQEFRE AATLVRDRLL
ELDPDMIAVD ALSPNLVTGC RMTGLPWMFT VPCSPSLTAT RKSLFDPHPM GSRRQRTLMS
ALENLKLTIR ETYGNAIKKD LYARRALLKK EFGLNSMGFN ADSAIVPPLW KDRNCVGGIH
FNTPGLWDSI RQPHQITFVG CGVTSDPENH SPSQAGTPIS EIAGWSPLTK LSTSFDQSGQ
GERDLDVEWM DAAYAAGESV VYLNMGSMFL WTDDEVRACL RAFERLHRES GGKIKLLFKL
NKPKRNPGSP GFTSPLNSPT AVATPKWDEK RPIDSRRPSG VSTLIMAEKL SEAIKNVKPR
RKTDAEKGYS QFMLSEFEGL EYVRFTRWVH DQRRIYKHPA LRVVIHHGGG NSFNEAVHYG
LPQMILSQWF DTHEYAILAE RFGIGLRSKH APFVDEQDMF AKMLRLLRGP EAEKIQANAK
IWSTRSRNAG GAPAAARLLE THALLHRQRK QARDPTPTAK TSLSVDTTEV ATPTFTDTET
SLSPKILSSA ASTVTNP
