UGT1_USTMA
ID UGT1_USTMA Reviewed; 578 AA.
AC A0A0D1CFF0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Glycosyltransferase ugt1 {ECO:0000303|PubMed:17850255};
DE EC=2.4.1.- {ECO:0000305|PubMed:17850255};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein ugt1 {ECO:0000303|PubMed:17850255};
GN Name=ugt1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06467;
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: Glycosyltransferase; part of the gene cluster that mediates
CC the 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 UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CM003162; KIS65763.1; -; Genomic_DNA.
DR RefSeq; XP_011392734.1; XM_011394432.1.
DR AlphaFoldDB; A0A0D1CFF0; -.
DR SMR; A0A0D1CFF0; -.
DR STRING; 237631.A0A0D1CFF0; -.
DR EnsemblFungi; KIS65763; KIS65763; UMAG_06467.
DR GeneID; 23566048; -.
DR KEGG; uma:UMAG_06467; -.
DR VEuPathDB; FungiDB:UMAG_06467; -.
DR eggNOG; KOG1192; Eukaryota.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..578
FT /note="Glycosyltransferase ugt1"
FT /id="PRO_0000452763"
FT REGION 81..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 64072 MW; 5DBD21779098B493 CRC64;
MATEHILLVC WPAVGHARPM LDYAAAQLKQ NPGLIITFIC SKMQIALLEG LAISEHLADK
KFGDRLRLLG TGRPAQEVLK EFGDREDAKN AANSASKAPN TTANGPEPEV ILTMQAATLI
QKRFAEIFPT ILANDDLFDE QDNSLLLPAC VAGKPTTIVV NWMLPGMVET VRKHSSDLKM
VTFFDNSCTF VTRMLGPRSI GGFGGIERLW SQYCNSNPEV DPNDSTLKEK LLGRRWTGKF
YIPGSRMGAI EEQEMAALAK DWLLSVPLTP SLIEIQKLVD ASHTILINTH LAVEERELDY
LRMVYPFKKI GILGPAMFSG FVEKGEKLAA KLLDKHINVK PAASRPLTPP ETPPPGSPDT
DSHGEEEDPK QKSVKQVEKF LAESATGSVV YISFGTMFRP QPTHLIKMLE IIIYEMSLSS
QFRLLFTFGG SKDLASSCPP SFAPQISALE SQLFKSGNTL FVNWVDQHYV LQHPSVGWFL
SHGGWNSCQE SMLAGTPLLI LPFFGDQLFN AYFLESIQIA YRFNTAANMS VADFVASFRE
GITCTRPESE RGSQLTKNAK ELQLRLKGER ALAEVRLF
