AHD1_USTMA
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 25-MAY-2022, entry version 37.
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}.
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DR EMBL; CM003162; KIS65765.1; -; Genomic_DNA.
DR RefSeq; XP_011392763.1; XM_011394461.1.
DR AlphaFoldDB; A0A0D1DT68; -.
DR STRING; 5270.UM06469P0; -.
DR EnsemblFungi; KIS65765; KIS65765; UMAG_12340.
DR GeneID; 23568085; -.
DR KEGG; uma:UMAG_12340; -.
DR VEuPathDB; FungiDB:UMAG_12340; -.
DR eggNOG; KOG0873; Eukaryota.
DR OrthoDB; 1321777at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C: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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:UniProt.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
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
