ID   UAT1_USTMA              Reviewed;         513 AA.
AC   A0A0D1CFE5;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Acyltransferase uat1 {ECO:0000303|PubMed:17850255};
DE            EC=2.3.1.- {ECO:0000305|PubMed:17850255};
DE   AltName: Full=Ustilagic acid biosynthesis cluster protein uat1 {ECO:0000303|PubMed:17850255};
GN   Name=uat1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06462;
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   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   [4]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=17850255; DOI=10.1111/j.1365-2958.2007.05941.x;
RA   Teichmann B., Linne U., Hewald S., Marahiel M.A., Boelker M.;
RT   "A biosynthetic gene cluster for a secreted cellobiose lipid with
RT   antifungal activity from Ustilago maydis.";
RL   Mol. Microbiol. 66:525-533(2007).
RN   [5]
RP   INDUCTION.
RX   PubMed=20173069; DOI=10.1128/aem.02211-09;
RA   Teichmann B., Liu L., Schink K.O., Boelker M.;
RT   "Activation of the ustilagic acid biosynthesis gene cluster in Ustilago
RT   maydis by the C2H2 zinc finger transcription factor Rua1.";
RL   Appl. Environ. Microbiol. 76:2633-2640(2010).
CC   -!- FUNCTION: Acyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of the glycolipid biosurfactant ustilagic acid (UA)
CC       (PubMed:15932999, PubMed:17850255). UA is a secreted cellobiose
CC       glycolipid that is toxic for many microorganisms and confers biocontrol
CC       activity to U.maydis (PubMed:15932999, PubMed:17850255). UA consists of
CC       15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-
CC       glycosidically linked to cellobiose at its terminal hydroxyl group
CC       (PubMed:17850255). In addition, the cellobiose moiety is acetylated and
CC       acylated with a short-chain hydroxy fatty acid (PubMed:17850255). UA
CC       biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed
CC       by the cytochrome P450 monooxygenase cyp1 (PubMed:17850255). Terminal
CC       hydroxylation of palmitic acid precedes subterminal hydroxylation
CC       catalyzed by the cytochrome P450 monooxygenase cyp2 (PubMed:17850255).
CC       Sequential glucosylation of the hydroxy fatty acid is probably
CC       catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose
CC       lipid is further decorated by acetylation of the proximal glucose
CC       residue and by acylation with a short-chain beta-hydroxy fatty acid at
CC       the distal glucose residue (Probable). The acyltransferase uat1 may be
CC       a good candidate for catalyzing either acetylation or acylation of the
CC       cellobiose lipid (Probable). The fatty acid synthase fas2 may be
CC       involved in synthesis of the carbon backbone of the short-chain beta-
CC       hydroxy fatty acid esterified to the cellobiose disaccharide
CC       (Probable). The secreted UA consists of a mixture of both alpha-
CC       hydroxylated and non-hydroxylated glycolipids; therefore, alpha-
CC       hydroxylation of the long-chain fatty, catalyzed by the fatty acid
CC       hydroxylase ahd1, occurs late in UA biosynthesis and may be the last
CC       step before secretion (PubMed:17850255). {ECO:0000269|PubMed:15932999,
CC       ECO:0000269|PubMed:17850255, ECO:0000305|PubMed:17850255}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:17850255}.
CC   -!- INDUCTION: Expression is strongly induced under conditions of nitrogen
CC       starvation (PubMed:17850255). Expression is positively regulated by the
CC       cluster-specific transcription factor rua1 that recognizes and binds to
CC       the specific 5'-T/G-G/T-C-G-C-A-T-A/T-C/T-C/T-G/A-3' upstream
CC       activating sequence found in all promoters of the UA biosynthesis genes
CC       (PubMed:20173069). {ECO:0000269|PubMed:17850255,
CC       ECO:0000269|PubMed:20173069}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; CM003162; KIS65758.1; -; Genomic_DNA.
DR   RefSeq; XP_011392730.1; XM_011394428.1.
DR   AlphaFoldDB; A0A0D1CFE5; -.
DR   SMR; A0A0D1CFE5; -.
DR   EnsemblFungi; KIS65758; KIS65758; UMAG_06462.
DR   GeneID; 23566044; -.
DR   KEGG; uma:UMAG_06462; -.
DR   VEuPathDB; FungiDB:UMAG_06462; -.
DR   eggNOG; ENOG502SA09; Eukaryota.
DR   OMA; WIATNDA; -.
DR   OrthoDB; 1130893at2759; -.
DR   Proteomes; UP000000561; Chromosome 23.
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   2: Evidence at transcript level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..513
FT                   /note="Acyltransferase uat1"
FT                   /id="PRO_0000452761"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ   SEQUENCE   513 AA;  56827 MW;  3D6669CFD2C389E2 CRC64;
     MVVKRILPLP RPAGLAPPTE VPLDGQDLAM PKMVMHCIWF FLASSQPSLE STSLQELEQA
     FTLGMQLFLA RFPAAGARTR HDKDTARWYL EYNDQGADLE VIQLDRPLQD DWKALDGKCD
     SVFAPRPVMI FDDDASIFSI KVTRLSCGSV AISTSTHHWL VDFVGYIDLM EELSHCVSIF
     LNDPNAQINI DEGATKFDWS RDLLAYSKQL EPESIPSATW FTERGSPPQM TRAPSSCHYA
     SLLFTQESLE KLKRSLAEWA LETAPTTATD RIVPSKDNWI ATNDALHALL WAAITDARGL
     DLNATTQLHT PLDGRRLLSS LSSADSQSRG KYIGNVHPGH VFPLPSSVVS AKDRSGLFNL
     AWLIRTQYLN VTPGQMSAII RHHNYTDAET FGPGRLPKCT SMFGNDVTIS NVARIPVRQR
     LDFGEKLGKP YTLTVVGMVP VTLNGLTLDS ADGTCFIIQA PAEWTSKEAV LQHQPRSGDN
     QAPGGMLVYV GMRSEEMDKL LQNSLLQEFA LVL