ID   MAC1_PSEA3              Reviewed;         552 AA.
AC   M9LYJ5;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Acyl-CoA-dependent acyltransferase MAC1 {ECO:0000303|PubMed:23558529};
DE            EC=2.-.-.- {ECO:0000250|UniProtKB:A0A0D1E3S6};
DE   AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein MAC1 {ECO:0000303|PubMed:31923270};
GN   Name=MAC1 {ECO:0000303|PubMed:23558529}; ORFNames=PANT_19d00003;
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:A0A0D1E3S6,
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 trichothecene O-acetyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DF196785; GAC75889.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LYJ5; -.
DR   SMR; M9LYJ5; -.
DR   STRING; 1151754.M9LYJ5; -.
DR   EnsemblFungi; GAC75889; GAC75889; PANT_19d00003.
DR   OrthoDB; 868865at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..552
FT                   /note="Acyl-CoA-dependent acyltransferase MAC1"
FT                   /id="PRO_0000449535"
SQ   SEQUENCE   552 AA;  60878 MW;  E2E8E07869166F91 CRC64;
     MSAQNGYEWQ QTERDVWTRT CLGHEAAASF NENIAYGHTE LSVTATFRVH HPASSGIAGT
     DQEQEDLVAR VRDAWIRTRY LRPEVAVEMT THTDASIPQA FTYRVLRDEV SLRRWVDQTM
     AVVRLGEPGA ESLEEVCAYT YNRALPTPGK QSMLYLVLPR LADEKDRNAH FVWNVSHALA
     DGGSISELYN VLLQAMIDAS PSTDGSVYIP SDQELDVLPL LPRSVVAAYR QQHKPSAADE
     EAAAETARDN LRLIQAKMNE SLALQPVTNW TTRKHETICI RRDIEADEAR ELIKFGKHIK
     SGVTYLASAA TVLATAETFP ERKASSTGAL MGMVRNARRW LSTEPVEGAT GNRTPLGSDA
     VFLWIPVDTQ KSLEPSFDGV PELVSVAARI RSELNKHLVS PHCISSYPVV AEFAQGALTN
     HWAEIEGANR SAHTPNAEEL SKIIGPQAPG FSSVGALQVH SRFEPASPSA RASGLWLERT
     DSAHRGRQVN ASPWISMLMI DGKIKLQLGF DAKFHDADKM EQWMQRTYEW LLVCAAAASS
     SVGTVAPISA RL