MAT1_PSEA3
ID MAT1_PSEA3 Reviewed; 520 AA.
AC M9LRQ6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Acetyltransferase MAT1 {ECO:0000303|PubMed:23558529};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:A0A0D1CRC9};
DE AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein MAT1T1 {ECO:0000303|PubMed:31923270};
GN Name=MAT1 {ECO:0000303|PubMed:23558529}; ORFNames=PANT_19c00002;
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 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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION.
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 [8]
RP FUNCTION, 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: Acyl-CoA-dependent acyltransferase; 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 (Probable) (PubMed:20564650, PubMed:31923270).
CC Depending on the number of acetyl groups, mannosylerythritol lipids can
CC be differentiated into MEL A (fully acetylated), MEL B and MEL C
CC (monoacetylated at R-6 and R-4, respectively), and the fully
CC deacetylated MEL D (By similarity). The first step in the pathway is
CC the generation of mannosylerythritol by the glycosyltransferase EMT1
CC which catalyzes the transfer of GDP-mannose to the C-4 atom of meso-
CC erythritol (Probable). This reaction has to be stereospecific, since
CC only mannosyl-D-erythritol is generated (Probable). The produced
CC disaccharide is subsequently acylated with fatty acids of various
CC lengths by the acyltransferases MAC1 and MAC2 at positions C-2 and C-3,
CC repectively (Probable). The existence of MEL derivatives which carry an
CC acetyl group at C-2 implies that at least MAC1 also accepts acetyl-CoA
CC as a donor (Probable). The final step of MEL biosynthesis is the
CC acetylation of the fully acylated mannosylerythritol lipids catalyzed
CC by the acetyl-CoA-dependent acetyltransferase MAT1 (Probable). MAT1
CC displays a relaxed regioselectivity and is able to transfer
CC acetylgroups to both positions C-4 and C-6 of the mannosyl moiety
CC (Probable). {ECO:0000250|UniProtKB:A0A0D1CRC9,
CC ECO:0000269|PubMed:20564650, ECO:0000269|PubMed:31923270,
CC ECO:0000305|PubMed:23558529, ECO:0000305|PubMed:31923270}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|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 -!- 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.6}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; DF196785; GAC75891.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LRQ6; -.
DR STRING; 1151754.M9LRQ6; -.
DR EnsemblFungi; GAC75891; GAC75891; PANT_19c00002.
DR OrthoDB; 643224at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..520
FT /note="Acetyltransferase MAT1"
FT /id="PRO_0000449540"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT ACT_SITE 456
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 520 AA; 57208 MW; 10440967111FC9AE CRC64;
MPATPPMPGY DAVAVPVLDS TLGNTDIMTR ISLTFPTQLS LALLQDSWYE LVRAWPILAA
RVRHTPSTPS GLSFLIPQPD KVKELEQRSR TSHKDQEKHI VIVDASSRSI ASFHPITAKA
IQSSLSRDTV SVGAAPDNAD SLKMTCSNAT TSLKQLLRAD QAYITAHATV WSDATTIALA
FSHIAGDAFS VKAIFEAWRQ TIESAAPAPL QGVGVDPFIT YLPPHGKNSK SEDTDKQGER
DVGLPLGFFQ YGFIDKVRLA WNLISDIKIK RPEKKFGQYY MYMPEEKVQA LMAQARADVD
ALVSASDDSE KQALDTRIST FNVLLAWLLQ NIHAANPKRK RMSTVMTIVN AKTRPPARHD
PSDYPPHQLW GGALGVPLEP LASGDYASLP LGQLALHIRT SLTAQIDPAN MQANIVTLLR
HTRWAKPSGK LIFFARPNHY LSGCTEWRST RFGELDFGAA ASPPSSVKPV AIGTDMEIAV
SKRNRWVIFG DMGGGVWFSG FMTDHEATHR DGFGRYQHVQ
