EMT1_USTMA
ID EMT1_USTMA Reviewed; 615 AA.
AC A0A0D1DZV5;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Erythritol-mannosyl-transferase 1 {ECO:0000303|PubMed:15932999};
DE EC=2.4.1.- {ECO:0000269|PubMed:15932999};
DE AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein EMT1 {ECO:0000303|PubMed:16885300};
GN Name=EMT1 {ECO:0000303|PubMed:15932999}; ORFNames=UMAG_03117;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15932999; DOI=10.1128/aem.71.6.3033-3040.2005;
RA Hewald S., Josephs K., Boelker M.;
RT "Genetic analysis of biosurfactant production in Ustilago maydis.";
RL Appl. Environ. Microbiol. 71:3033-3040(2005).
RN [5]
RP FUNCTION, AND PATHWAY.
RX PubMed=16885300; DOI=10.1128/aem.00506-06;
RA Hewald S., Linne U., Scherer M., Marahiel M.A., Kaemper J., Boelker M.;
RT "Identification of a gene cluster for biosynthesis of mannosylerythritol
RT lipids in the basidiomycetous fungus Ustilago maydis.";
RL Appl. Environ. Microbiol. 72:5469-5477(2006).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24835306; DOI=10.1111/mmi.12642;
RA Freitag J., Ast J., Linne U., Stehlik T., Martorana D., Boelker M.,
RA Sandrock B.;
RT "Peroxisomes contribute to biosynthesis of extracellular glycolipids in
RT fungi.";
RL Mol. Microbiol. 93:24-36(2014).
RN [11]
RP FUNCTION.
RX PubMed=31103599; DOI=10.1016/j.fgb.2019.05.003;
RA Deinzer H.T., Linne U., Xie X., Boelker M., Sandrock B.;
RT "Elucidation of substrate specificities of decorating enzymes involved in
RT mannosylerythritol lipid production by cross-species complementation.";
RL Fungal Genet. Biol. 130:91-97(2019).
CC -!- FUNCTION: Erythritol-mannosyl-transferase; part of the gene cluster
CC that mediates the biosynthesis of mannosylerythritol lipids (MELs),
CC surface-active substances that enhance the availability of water-
CC insoluble substrates (PubMed:15932999, PubMed:16885300).
CC Mannosylerythritol lipid production is responsible for hemolytic
CC activity of Ustilago maydis (PubMed:15932999). 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 (PubMed:31103599).
CC The first step in the pathway is the generation of mannosylerythritol
CC by the glycosyltransferase EMT1 which catalyzes the transfer of GDP-
CC mannose to the C-4 atom of meso-erythritol (PubMed:15932999). This
CC reaction has to be stereospecific, since only mannosyl-D-erythritol is
CC generated (PubMed:15932999). The produced disaccharide is subsequently
CC acylated with fatty acids of various lengths derived from the
CC peroxisomal beta-oxidation by the peroxisomal acyltransferases MAC1 and
CC MAC2 at positions C-2 and C-3, repectively (PubMed:16885300,
CC PubMed:24835306, PubMed:31103599). The existence of MEL derivatives
CC which carry an acetyl group at C-2 implies that at least MAC1 also
CC accepts acetyl-CoA as a donor (PubMed:15932999). The final step of MEL
CC biosynthesis is the acetylation of the fully acylated
CC mannosylerythritol lipids catalyzed by the acetyl-CoA-dependent
CC acetyltransferase MAT1 (PubMed:16885300). 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 (PubMed:15932999).
CC {ECO:0000269|PubMed:15932999, ECO:0000269|PubMed:16885300,
CC ECO:0000269|PubMed:24835306, ECO:0000269|PubMed:31103599}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:15932999}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:24835306};
CC Peripheral membrane protein {ECO:0000305|PubMed:24835306}.
CC -!- INDUCTION: Expression is induced under conditions of nitrogen
CC starvation. {ECO:0000269|PubMed:15932999}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of mannosylerythritol
CC lipids (MELs) and leads the sticking of cells to each other in
CC hydrophobic environment (PubMed:15932999). Does not affect the
CC virulence (PubMed:15932999). {ECO:0000269|PubMed:15932999}.
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.9}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CM003146; KIS69146.1; -; Genomic_DNA.
DR RefSeq; XP_011389468.1; XM_011391166.1.
DR AlphaFoldDB; A0A0D1DZV5; -.
DR EnsemblFungi; KIS69146; KIS69146; UMAG_03117.
DR GeneID; 23563678; -.
DR KEGG; uma:UMAG_03117; -.
DR VEuPathDB; FungiDB:UMAG_03117; -.
DR eggNOG; ENOG502QUA1; Eukaryota.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000000561; Chromosome 7.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase; Vacuole.
FT CHAIN 1..615
FT /note="Erythritol-mannosyl-transferase 1"
FT /id="PRO_0000449532"
FT REGION 366..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 68132 MW; 98D96D9559972236 CRC64;
MKVALLANPA RGEINVLLAT AYELIRLGHD VTFLTGSSFA NAIAEFRSEQ NDPILAARIH
FSDLGNARAV EDFTRGMQSH LKGLRKPPGD YSSMEICQIV ALVTEQEFRD AATMVRDRLL
EIEPDMIAVD ALSPNLVTGC RMTGLPWMFT VPCSPSLTAT RKSLFDPHPM GRRRQRTLMS
ALENLKLTFI ETYRNATKKD LYARRALLKN EFGLNSMGFN GDSAIVPPLW KDRNCVGGIH
FNTPGLTDSI RQPHQIHFVG AGVTSDPENH DTPVFEAASF LKQLSPSSST TFKPLFPPLS
KTGRDLDVEW MDEAYAAGQL VVYLNMGSMF LWTDAEVRSC LRAFERLYEQ SGGKIKLLFK
LNKPKRTPNN TGASTPTAPI SSPDFEEKQR TVMGSARPVG ASNLVSEKLA DAIKNVTPRR
KTDADKGYSQ FTLSEFEGLE YVRFTRWVHD QRSIYKHPAL RVVIHHGGGN SFNEAVHYAL
PQMILSQWFD THEYAILAER FGIGLRSKHA PKIDENDLVN TMTRLLQGPE AEKIRRNAKV
WSIRSRNAGG APAAARLIEA QAMLFNQQKQ LELAASEVRA AVDTLSGKSS VADLESETAF
TPNMLSGAAS TVGSD
