ID   ORF1_USTMA              Reviewed;         429 AA.
AC   A0A0D1DT65;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Probable alcohol acetyltransferase orf1 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000305|PubMed:17850255};
DE   AltName: Full=Ustilagic acid biosynthesis cluster protein orf1 {ECO:0000303|PubMed:17850255};
GN   Name=orf1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06464;
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: Probable alcohol acetyltransferase; part of the gene cluster
CC       that mediates the biosynthesis of the glycolipid biosurfactant
CC       ustilagic acid (UA) (PubMed:15932999, PubMed:17850255). UA is a
CC       secreted cellobiose glycolipid that is toxic for many microorganisms
CC       and confers biocontrol activity to U.maydis (PubMed:15932999,
CC       PubMed:17850255). UA consists of 15,16-dihydroxypalmitic or 2,15,16-
CC       trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose
CC       at its terminal hydroxyl group (PubMed:17850255). In addition, the
CC       cellobiose moiety is acetylated and acylated with a short-chain hydroxy
CC       fatty acid (PubMed:17850255). UA biosynthesis starts with omega-
CC       hydroxylation of palmitic acid catalyzed by the cytochrome P450
CC       monooxygenase cyp1 (PubMed:17850255). Terminal hydroxylation of
CC       palmitic acid precedes subterminal hydroxylation catalyzed by the
CC       cytochrome P450 monooxygenase cyp2 (PubMed:17850255). Sequential
CC       glucosylation of the hydroxy fatty acid is probably catalyzed by the
CC       glycosyltransferase ugt1 (Probable). The cellobiose lipid is further
CC       decorated by acetylation of the proximal glucose residue and by
CC       acylation with a short-chain beta-hydroxy fatty acid at the distal
CC       glucose residue (Probable). The acyltransferase uat1 may be a good
CC       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 alcohol acetyltransferase FCK4 family.
CC       {ECO:0000305}.
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DR   EMBL; CM003162; KIS65760.1; -; Genomic_DNA.
DR   RefSeq; XP_011392731.1; XM_011394429.1.
DR   AlphaFoldDB; A0A0D1DT65; -.
DR   SMR; A0A0D1DT65; -.
DR   EnsemblFungi; KIS65760; KIS65760; UMAG_06464.
DR   GeneID; 23566045; -.
DR   KEGG; uma:UMAG_06464; -.
DR   VEuPathDB; FungiDB:UMAG_06464; -.
DR   OrthoDB; 1787980at2759; -.
DR   Proteomes; UP000000561; Chromosome 23.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..429
FT                   /note="Probable alcohol acetyltransferase orf1"
FT                   /id="PRO_0000452765"
SQ   SEQUENCE   429 AA;  47532 MW;  114C063CC81BDF2B CRC64;
     MPSRIPSSND PVLPGRELWG TERFWHFAHH EHQGAFDMVS IFVVDVGSRH LSIEDWRKAW
     SKLYRTFAVL SQKISDDSGE GKIVDGALRA EESFFTGPIL QDDQDRIDYS LQQRRFDCLS
     LTVFATSGTE HESFHLAISN PHALGDAKGI FAIGKALIQG VLSQTQAELQ SPTSPPPQPS
     LKAFTTSHNQ DLGLKAMFEV ARTGSSIGFP ILPKETSAEL EPASREWRRV FTFSPAQTET
     LVQLCKAKAL TVSAWLQATI LHALIDTLVD DKGDEKAEQT FTVAAMPFHS PLSVSGATST
     IFAPISIRVG SKAELNDIAE AVAESFGLAR RFAEDVQDDY VKTLLKLFGS VRLETSVPTF
     SSLGRLDTVT GLKRYHVVAR NNLPTTGIHA WTLNDQLNLT LSWAPARFRR DHIEKFWSTW
     IGTIKEVVA