ID AHD1_USTMA Reviewed; 383 AA. AC A0A0D1DT68; DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2015, sequence version 1. DT 24-JAN-2024, entry version 43. DE RecName: Full=Fatty acid hydroxylase ahd1 {ECO:0000303|PubMed:17850255}; DE EC=1.-.-.- {ECO:0000269|PubMed:17850255}; DE AltName: Full=Ustilagic acid biosynthesis cluster protein ahd1 {ECO:0000303|PubMed:17850255}; GN Name=ahd1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_12340; 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, DISRUPTION PHENOTYPE, 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:0000269|PubMed:17850255}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane CC protein {ECO:0000255}. 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 -!- DISRUPTION PHENOTYPE: Leads to the production of UA derivatives that CC lack the alpha-hydroxyl group. {ECO:0000269|PubMed:17850255}. CC -!- SIMILARITY: Belongs to the sterol desaturase family. {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; KIS65765.1; -; Genomic_DNA. DR RefSeq; XP_011392763.1; XM_011394461.1. DR AlphaFoldDB; A0A0D1DT68; -. DR STRING; 237631.A0A0D1DT68; -. DR GlyCosmos; A0A0D1DT68; 1 site, No reported glycans. DR EnsemblFungi; KIS65765; KIS65765; UMAG_12340. DR GeneID; 23568085; -. DR KEGG; uma:UMAG_12340; -. DR VEuPathDB; FungiDB:UMAG_12340; -. DR eggNOG; KOG0873; Eukaryota. DR InParanoid; A0A0D1DT68; -. DR OrthoDB; 374293at2759; -. DR Proteomes; UP000000561; Chromosome 23. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR PANTHER; PTHR11863:SF226; FATTY ACID HYDROXYLASE DOMAIN-CONTAINING PROTEIN 2-RELATED; 1. DR PANTHER; PTHR11863; STEROL DESATURASE; 1. DR Pfam; PF04116; FA_hydroxylase; 1. PE 2: Evidence at transcript level; KW Glycoprotein; Membrane; Oxidoreductase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..383 FT /note="Fatty acid hydroxylase ahd1" FT /id="PRO_0000452764" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 123..143 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 214..236 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 217..341 FT /note="Fatty acid hydroxylase" FT /evidence="ECO:0000255" FT CARBOHYD 342 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 383 AA; 43603 MW; 449B7008B1729EEC CRC64; MTTRTATSTS TTVHGHLGDL KLRNAAITGP HLQPKAAKQD LADTKPDSAR TFPGLGFKLS PTEERLRAKR NWGFLETAYD NSKVMGLTTH FVTITMAIVF NKSWLAKPVY DWLNTYDRFT IHTVHTWILL STCQLLVIGL FALTDLSGRP SWLARYRMQP HKPPTLAQYK KLIPVVLFNL VVVNTISNII YYPLAEWRGI QTTYETLPSG KKLVAQWLVC LLMEDIGFYT VHRALHHPRI YKYIHKKHHE FSAPIAGAST YAHPLEHYFS NLVPILVGLL ITRAHISVQY LFFTGLMIGS HVQHSGYNIP FLTCALVHDW HHYFNTENYG PVGLLDAIFK TNKTFKAWTS ETVAAFHGDR AKARQAALEK LAQIEAEEQE RIR //