UHD1_USTMA
ID UHD1_USTMA Reviewed; 300 AA.
AC A0A0D1BUI1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Fatty acid hydroxylase uhd1 {ECO:0000303|PubMed:17850255};
DE EC=1.-.-.- {ECO:0000305|PubMed:17850255};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein uhd1 {ECO:0000303|PubMed:17850255};
GN Name=uhd1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06466;
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: Fatty acid hydroxylase; part of the gene cluster that
CC mediates the biosynthesis of the glycolipid biosurfactant ustilagic
CC acid (UA) (PubMed:15932999, PubMed:17850255). UA is a secreted
CC cellobiose glycolipid that is toxic for many microorganisms and confers
CC biocontrol activity to U.maydis (PubMed:15932999, PubMed:17850255). UA
CC consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid,
CC which is O-glycosidically linked to cellobiose at its terminal hydroxyl
CC group (PubMed:17850255). In addition, the cellobiose moiety is
CC acetylated and acylated with a short-chain hydroxy fatty acid
CC (PubMed:17850255). UA biosynthesis starts with omega-hydroxylation of
CC palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1
CC (PubMed:17850255). Terminal hydroxylation of palmitic acid precedes
CC subterminal hydroxylation catalyzed by the cytochrome P450
CC monooxygenase cyp2 (PubMed:17850255). Sequential glucosylation of the
CC hydroxy fatty acid is probably catalyzed by the glycosyltransferase
CC ugt1 (Probable). The cellobiose lipid is further decorated by
CC acetylation of the proximal glucose residue and by acylation with a
CC short-chain beta-hydroxy fatty acid at the distal glucose residue
CC (Probable). The acyltransferase uat1 may be a good candidate for
CC catalyzing either acetylation or acylation of the cellobiose lipid
CC (Probable). The fatty acid synthase fas2 may be involved in synthesis
CC of the carbon backbone of the short-chain beta-hydroxy fatty acid
CC esterified to the cellobiose disaccharide (Probable). The secreted UA
CC consists of a mixture of both alpha-hydroxylated and non-hydroxylated
CC glycolipids; therefore, alpha-hydroxylation of the long-chain fatty,
CC catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA
CC biosynthesis and may be the last step before secretion
CC (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 NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003162; KIS65762.1; -; Genomic_DNA.
DR RefSeq; XP_011392733.1; XM_011394431.1.
DR AlphaFoldDB; A0A0D1BUI1; -.
DR SMR; A0A0D1BUI1; -.
DR STRING; 5270.UM06466P0; -.
DR EnsemblFungi; KIS65762; KIS65762; UMAG_06466.
DR GeneID; 23566047; -.
DR KEGG; uma:UMAG_06466; -.
DR VEuPathDB; FungiDB:UMAG_06466; -.
DR eggNOG; KOG1502; Eukaryota.
DR OrthoDB; 848823at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..300
FT /note="Fatty acid hydroxylase uhd1"
FT /id="PRO_0000452762"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 14..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 63..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 83..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 183..186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ SEQUENCE 300 AA; 32873 MW; 7396A2FAD60F4EA2 CRC64;
MAGTSRNVRV LVTGANGFVG SHIVSLLLSR GYVVNATVRR QTASEKLIAT FACDRLHVFV
IPDLTSEQAL DEAIRGCKYV VHVASTVPSK EQASGIDIDS AISSIESVMN SAVAHASEKV
VLTSSMSTHL DVKAPILNES TWYTPDRSST KLMVQYMSSK TLVERRAWEL SSTLKLPLTT
VAPVYIGGPT IIHEQDPKSS VSNQDLLRCI EDESRSRIPG WIDVRTVAHL HLHAIEDHSL
NGRRILACTH NRGVVPMDCS LMNSLLAKDS AALIDFDRTK RDLLEQIDAF NSGQTRRVVA
