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MAC1_USTMA
ID   MAC1_USTMA              Reviewed;         591 AA.
AC   A0A0D1E3S6;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Acyl-CoA-dependent acyltransferase MAC1 {ECO:0000303|PubMed:16885300};
DE            EC=2.-.-.- {ECO:0000269|PubMed:16885300};
DE   AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein MAC1 {ECO:0000303|PubMed:16885300};
GN   Name=MAC1 {ECO:0000303|PubMed:16885300}; ORFNames=UMAG_03116;
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.
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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, 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, FUNCTION, AND DOMAIN.
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, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
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: 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 (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:16885300}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24835306}.
CC   -!- DOMAIN: The C-terminal PTS1-type tripeptide peroxisomal targeting
CC       signal is required for the import into peroxisomes.
CC       {ECO:0000269|PubMed:24835306}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes completely the production of
CC       mannosylerythritol lipids (MELs). {ECO:0000269|PubMed:16885300}.
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 trichothecene O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CM003146; KIS69145.1; -; Genomic_DNA.
DR   RefSeq; XP_011389467.1; XM_011391165.1.
DR   AlphaFoldDB; A0A0D1E3S6; -.
DR   SMR; A0A0D1E3S6; -.
DR   EnsemblFungi; KIS69145; KIS69145; UMAG_03116.
DR   GeneID; 23563677; -.
DR   KEGG; uma:UMAG_03116; -.
DR   VEuPathDB; FungiDB:UMAG_03116; -.
DR   eggNOG; ENOG502RYJG; Eukaryota.
DR   OMA; QINESPW; -.
DR   OrthoDB; 868865at2759; -.
DR   Proteomes; UP000000561; Chromosome 7.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR009992; Tri3/Sat12/Sat16/Mac1.
DR   Pfam; PF07428; Tri3; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Peroxisome; Reference proteome; Transferase.
FT   CHAIN           1..591
FT                   /note="Acyl-CoA-dependent acyltransferase MAC1"
FT                   /id="PRO_0000449534"
FT   REGION          589..591
FT                   /note="Peroxisomal targeting signal type 1"
FT                   /evidence="ECO:0000269|PubMed:24835306"
SQ   SEQUENCE   591 AA;  66282 MW;  6F84D9B60DC83D18 CRC64;
     MINNALRTLI SSATEQSLDD VLEHEFRTAV QLQQMDQFEW HQVEADLWKR TCLGHEASAS
     FNQNIAHGHT ELSLMTSWRV HQPSSSRITG SELELDQLVA RVRQAWIQAR YLRPEVGVEL
     DTHTDPTVAQ TMCYRLLRDE ESIQEWLDET FVVKRLGDPG VATPAELCAY TYNRPLATKG
     KKSMLYLILP RLDDEQRTAY TIWNVSHAVT DGGSLAEVFN TLFQCVIDAT PSEPYDSIYT
     PSAFELNVLP RMPRSVVMAY RQQYQPKPEE IAKAHKVAEV NMRMITEKMG ESLALMPSTS
     WPERKHETVC LCRELEANEV RELLKFAKQV HSGITYLASA ATILSAAETF PERKASSKGA
     LVGMVRNARR WISATPLDAS LGASTPLGSD AVFLWVPIDT HKTLEPSFSR MQELVTTARH
     IRHELDKHLT TPHCISSYPY VAESSIQGLN QQWSQIKAVQ SPSSSSSQKE IAGIIGAQAP
     GFSSVGMMRI RPRFEPVSAN ARASGLWLER TDFTHTGRQI NASPWISMFN VDGRIKLQLG
     FDTKFHEVEK MNQWLDRTVV WMRICAAAAA TTSTSVSSTS VDATAPVFAR L
 
 
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