CYP1_USTMD
ID CYP1_USTMD Reviewed; 435 AA.
AC E9RHV4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome P450 monooxygenase cyp1 {ECO:0000303|PubMed:22985214};
DE EC=1.-.-.- {ECO:0000269|PubMed:22985214};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein cyp1 {ECO:0000303|PubMed:22985214};
DE Flags: Fragment;
GN Name=cyp1 {ECO:0000303|PubMed:22985214};
OS Ustilago maydis (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=5270;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NBRC 7530;
RX PubMed=22985214; DOI=10.1111/1567-1364.12005;
RA Morita T., Fukuoka T., Imura T., Kitamoto D.;
RT "Accumulation of cellobiose lipids under nitrogen-limiting conditions by
RT two ustilaginomycetous yeasts, Pseudozyma aphidis and Pseudozyma
RT hubeiensis.";
RL FEMS Yeast Res. 13:44-49(2013).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
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 [3]
RP FUNCTION, 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 [4]
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the glycolipid biosurfactant ustilagic
CC acid (UA) (PubMed:15932999, PubMed:17850255, PubMed:22985214). UA is a
CC secreted cellobiose glycolipid that is toxic for many microorganisms
CC and confers biocontrol activity to U.maydis (PubMed:15932999,
CC PubMed:17850255, PubMed:22985214). UA consists of 15,16-
CC 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:0000269|PubMed:22985214,
CC ECO:0000305|PubMed:17850255}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17850255}.
CC -!- INDUCTION: Expression is strongly induced under conditions of nitrogen
CC starvation (PubMed:15932999). 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:15932999,
CC ECO:0000269|PubMed:20173069}.
CC -!- DISRUPTION PHENOTYPE: Results in complete loss of ustilagic acid
CC production. {ECO:0000269|PubMed:15932999}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB602450; BAJ78287.1; -; Genomic_DNA.
DR AlphaFoldDB; E9RHV4; -.
DR SMR; E9RHV4; -.
DR VEuPathDB; FungiDB:UMAG_11812; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN <1..>435
FT /note="Cytochrome P450 monooxygenase cyp1"
FT /id="PRO_0000452758"
FT BINDING 386
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 435
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 50132 MW; 5F9BB272075CDDF1 CRC64;
NTHTLPGLGR LIDVSRPDWI EHVQKTNFSN YVKGEQFHDQ MRDVLGDGIF TSDGERWKMQ
RKVASRIFTV SSFKAIITQT IREDCALVEK LIETYAKEGT VFNLQELYFK FTLSSFVKIA
FSQDIMSLSE PDRPDTFGDA FNYAQKVLDM RFVQPWWKIA ERFNETGRKM RAARKIVEEF
TNNIVEARRE ESDAMGEKSK PESGRKDLLD LFMGYRSSDG QRLSNQQLKD TILNLMIAGR
DTTAEALSWM SWHMLTKPEV YSRIRREIDT SLDEDGEQAG LEIDYDVFEQ HTAKLSTFQE
TLRLHPSIPK NIRRALKDDV LPNGGPRVRK GDLMLYSDWA MARNPDIWGP DACEFKPSRW
IDEETGSTVK YSQFQAHFFN GGPRLCLGQK LASYEVVQLI HHIFAKFDLE LVDLGPKKSA
GFDKVPDYLN SLTHP
