MAT1_USTMA
ID MAT1_USTMA Reviewed; 534 AA.
AC A0A0D1CRC9;
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=Acetyltransferase MATC1 {ECO:0000303|PubMed:16885300};
DE EC=2.3.1.- {ECO:0000269|PubMed:16885300};
DE AltName: Full=Mannosylerythritol lipids (MELs) biosynthesis cluster protein MAT1 {ECO:0000303|PubMed:16885300};
GN Name=MAT1 {ECO:0000303|PubMed:16885300}; ORFNames=UMAG_03114;
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, 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: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of mannosylerythritol lipids (MELs), surface-active
CC substances that enhance the availability of water-insoluble substrates
CC (PubMed:15932999, PubMed:16885300). Mannosylerythritol lipid production
CC is responsible for hemolytic activity of Ustilago maydis
CC (PubMed:15932999). Depending on the number of acetyl groups,
CC mannosylerythritol lipids can be differentiated into MEL A (fully
CC acetylated), MEL B and MEL C (monoacetylated at R-6 and R-4,
CC respectively), and the fully deacetylated MEL D (PubMed:31103599). 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: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: Cell membrane {ECO:0000269|PubMed:24835306};
CC Peripheral membrane protein {ECO:0000305|PubMed:24835306}.
CC -!- DISRUPTION PHENOTYPE: Leads to the secretion of large amounts of
CC deacetylated MEL D. {ECO:0000269|Ref.2}.
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 plant acyltransferase family. {ECO:0000305}.
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DR EMBL; CM003146; KIS69143.1; -; Genomic_DNA.
DR RefSeq; XP_011389465.1; XM_011391163.1.
DR AlphaFoldDB; A0A0D1CRC9; -.
DR EnsemblFungi; KIS69143; KIS69143; UMAG_03114.
DR GeneID; 23563675; -.
DR KEGG; uma:UMAG_03114; -.
DR VEuPathDB; FungiDB:UMAG_03114; -.
DR eggNOG; ENOG502RJXU; Eukaryota.
DR OMA; KRCTAFN; -.
DR OrthoDB; 643224at2759; -.
DR Proteomes; UP000000561; Chromosome 7.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase.
FT CHAIN 1..534
FT /note="Acetyltransferase MATC1"
FT /id="PRO_0000449539"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT ACT_SITE 459
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 534 AA; 58994 MW; A8E3B5F422C92CB6 CRC64;
MKSNVDTVLD GYTSVPVGVL DSTLANTDIL TRITLVFPSS LSLSALQESW YALVRSWPIL
AARVRATPST PSGLSYLIPT PATLESLETR SRNSASKPLE KHIVLLDQSS RSFSDYHPIV
AKAVHSNLDR NNISIGGAPL VEHEKATICS NACTSWKQLI KQDQAFVTAQ ATKFADATTV
TISFSHILGD AFTIKHIFQG WQTALNGQAV QELQDVGKDP FIKYLPKDTN DKKHKKNKKS
EPAPDLPLQW FRYGLARKIK LISLLLWEVK VKKPEKTLGQ YYIYLPQAKV DELMAQARSD
LEQLRSSSAT SATERDLNVS TFNVLFAWLL QNIHASTAIK PSKTSSVICI INAKTRPPAG
HVPADYPRHQ LWGGALGAPL RPLSAAEYVT LPLGQLALHI RESITEQVDP ENIRKSVVMA
LKHSMWKKPS GELLFFSQNP NTYWCGCTEW RSAKFHTIDF SAAATPHHDA IQPTAAPAAS
VNPVAITTNM ETPMTKRNRW ALLGEANNGI WFTGGLTANE ASNKNGFGRY IFVE
