CYP1_USTMA
ID CYP1_USTMA Reviewed; 640 AA.
AC A0A0D1DMJ7;
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=Cytochrome P450 monooxygenase cyp1 {ECO:0000303|PubMed:17850255};
DE EC=1.-.-.- {ECO:0000269|PubMed:17850255};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein cyp1 {ECO:0000303|PubMed:17850255};
GN Name=cyp1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_11812;
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, 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 [4]
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 [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).
RN [6]
RP FUNCTION.
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).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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; CM003162; KIS65759.1; -; Genomic_DNA.
DR RefSeq; XP_011392749.1; XM_011394447.1.
DR AlphaFoldDB; A0A0D1DMJ7; -.
DR SMR; A0A0D1DMJ7; -.
DR STRING; 5270.UM06463P0; -.
DR EnsemblFungi; KIS65759; KIS65759; UMAG_11812.
DR GeneID; 23567650; -.
DR KEGG; uma:UMAG_11812; -.
DR VEuPathDB; FungiDB:UMAG_11812; -.
DR eggNOG; KOG0157; Eukaryota.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..640
FT /note="Cytochrome P450 monooxygenase cyp1"
FT /id="PRO_0000452757"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 572
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 CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 640 AA; 73435 MW; F81C0C9D593CF7BB CRC64;
MRQRADVEVG PLKSGLLFSY MQNFCALQTR LRRPSRTTEL DTMDFKPFLT LQHFRPQGFA
GDVLAPGASY NQTWNTMASK FNGRGGNRVE TGKVLEAASE SLKETVPLLQ LVVRARHHPL
LVFLVGLFLG TIYLLYRYWD CAVGCERRPD LKGPKGLPLI GNLMWALKNR DPLSYQVYAQ
QKYGYGNTHT LPGLGRLIDI SRPDWIEHVQ KIKFSNYVKG EQFHDQMRDV LGDGIFTSDG
ERWKMQRKVA SRIFTVSSFK AIITQTIRED CALVEQLIET YARQGTVFNL QELYFKFTLS
SFVKIAFSQD IKSLSEPDRP DTFGDAFNYA QKVLDMRFVQ PWWKIAERFN ETGRKMRAAR
KIVEEFTTNI VEARRKESEA MGEKSKPESS RKDLLDLFMA YRSSDGQRLS NQQLKDTILN
LMIAGRDTTA EALSWMSWHM LTKPDVYDRI RHEIDATLEE EGEQAGLEID YDVFEQHTAK
LTTFQETLRL HPSIPKNIRR ALQDDVLPNG GPRVRKGDLM LYSDWAMGRN PDIWGPDACE
FKPSRWTDQE TGSSIKYSQF QAHFFNGGPR LCLGQKLASY EVVQLIHHIF AKFDLELIDL
GPGRSAGFGK VPDYLNSLTH PMKRPLMVKA TLRCCKEGTR
