ID   VLMA_LECSP              Reviewed;         365 AA.
AC   A0A024FA41;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Fatty acid hydroxylase vlmA {ECO:0000303|PubMed:24848421};
DE            EC=1.-.-.- {ECO:0000305|PubMed:24848421};
DE   AltName: Full=Verlamelin biosynthesis protein A {ECO:0000303|PubMed:24848421};
GN   Name=vlmA {ECO:0000303|PubMed:24848421};
OS   Lecanicillium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Lecanicillium;
OC   unclassified Lecanicillium.
OX   NCBI_TaxID=1756136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=HF627;
RX   PubMed=24848421; DOI=10.1007/s00253-014-5803-7;
RA   Ishidoh K., Kinoshita H., Nihira T.;
RT   "Identification of a gene cluster responsible for the biosynthesis of
RT   cyclic lipopeptide verlamelin.";
RL   Appl. Microbiol. Biotechnol. 98:7501-7510(2014).
CC   -!- FUNCTION: Fatty acid hydroxylase; part of the gene cluster that
CC       mediates the biosynthesis of verlamelin, a lipopeptide that exhibits
CC       antifungal activity against plant pathogenic fungi (PubMed:24848421).
CC       Verlamelin is a cyclic hexadepsipeptide and is bridged by ester bonding
CC       between a 5-hydroxytetradecanoic acid moiety and a carboxyl group on
CC       the terminal Val of amide-bonded tetradecanoyl-hexapeptide D-allo-Thr-
CC       D-Ala-L-Pro-L-Gln-D-Tyr-L-Val (PubMed:24848421). VlmA and vlmB are
CC       altogether regarded as essential components in the biosynthesis of 5-
CC       hydroxytetradecanoic acid (PubMed:24848421). VlmA catalyzes the
CC       hydroxylation at position C5 of tetradecanoic acid produced in primary
CC       metabolism, while the precise function of vlmB still remains to be
CC       solved (PubMed:24848421). To be loaded onto the waiting NRPS, 5-
CC       hydroxytetradecanoic acid is activated in the form of acyladenylate by
CC       the AMP-dependent ligase vlmC (PubMed:24848421). VlmS seems to accept
CC       the fatty-acyl intermediate onto the initial module to further elongate
CC       amino acid residues by the downstream modules (PubMed:24848421). In
CC       addition, in the last module at its C-terminus, vlmS contains a surplus
CC       condensation (C) domain that may be involved in cyclization, the last
CC       step to form verlamelin (PubMed:24848421).
CC       {ECO:0000269|PubMed:24848421}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:24848421}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to complete loss of verlamelin production
CC       (PubMed:24848421). {ECO:0000269|PubMed:24848421}.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. TMEM195 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB862313; BAO73253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024FA41; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IEA:UniProt.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Oxidoreductase; Transmembrane; Transmembrane helix;
KW   Virulence.
FT   CHAIN           1..365
FT                   /note="Fatty acid hydroxylase vlmA"
FT                   /id="PRO_0000438577"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          189..335
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   REGION          20..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   365 AA;  42640 MW;  3A293C0EC90860A9 CRC64;
     MPSTTQTTVQ SIDSIDSIPT TIKRRQNDKT KTPKTKPVSK IPICPKNSSI PRLDQPSQHK
     FILLQSLLPI TVHQLTTLVL SISRYDDYVH PFLLRLCVII GYGYAFRFLL RREGLAIRTL
     GKKLGYLDGD HHPRDKVPRD STRLNWSLPL TVGSRTVMCV LVAYDPSQQP INYLASLKWW
     AWLAVYLSLY PIILDFYYYC VHRAWHEVPC LWRFHRRHHT IKRPSILFTA YADSEQELFD
     IVGTPLLTFF TLKALHLPMD FYTWWICIQY IAYTEVMGHS GLRIYTTPPI SCSWLLQRFG
     VELVIEDHDL HHRQGYRQAR NYGKQTRIWD RLFGTCADRI ETNPVNIQKG RRVMMHSINI
     PSLGN