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CYPX_DOTSE
ID   CYPX_DOTSE              Reviewed;         511 AA.
AC   Q30DW6;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Cytochrome P450 monooxygenase cypX {ECO:0000303|PubMed:23207690};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23207690};
DE   AltName: Full=Dothistromin biosynthesis protein cypX {ECO:0000303|PubMed:23207690};
GN   Name=cypX {ECO:0000303|PubMed:23207690};
GN   Synonyms=cypA {ECO:0000303|PubMed:17683963};
OS   Dothistroma septosporum (Red band needle blight fungus) (Mycosphaerella
OS   pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=64363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=NZE7;
RX   PubMed=16649078; DOI=10.1007/s11046-006-0240-5;
RA   Bradshaw R.E., Jin H., Morgan B.S., Schwelm A., Teddy O.R., Young C.A.,
RA   Zhang S.;
RT   "A polyketide synthase gene required for biosynthesis of the aflatoxin-like
RT   toxin, dothistromin.";
RL   Mycopathologia 161:283-294(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=NZE7;
RX   PubMed=17683963; DOI=10.1016/j.fgb.2007.06.005;
RA   Zhang S., Schwelm A., Jin H., Collins L.J., Bradshaw R.E.;
RT   "A fragmented aflatoxin-like gene cluster in the forest pathogen
RT   Dothistroma septosporum.";
RL   Fungal Genet. Biol. 44:1342-1354(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NZE1 / ATCC MYA-605;
RA   Zhang S., Bradshaw R.E.;
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=12039746; DOI=10.1128/aem.68.6.2885-2892.2002;
RA   Bradshaw R.E., Bhatnagar D., Ganley R.J., Gillman C.J., Monahan B.J.,
RA   Seconi J.M.;
RT   "Dothistroma pini, a forest pathogen, contains homologs of aflatoxin
RT   biosynthetic pathway genes.";
RL   Appl. Environ. Microbiol. 68:2885-2892(2002).
RN   [5]
RP   REVIEW ON FUNCTION, AND PATHWAY.
RX   PubMed=22069571; DOI=10.3390/toxins2112680;
RA   Schwelm A., Bradshaw R.E.;
RT   "Genetics of dothistromin biosynthesis of Dothistroma septosporum: an
RT   update.";
RL   Toxins 2:2680-2698(2010).
RN   [6]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=23207690; DOI=10.1016/j.fgb.2012.11.006;
RA   Chettri P., Ehrlich K.C., Cary J.W., Collemare J., Cox M.P.,
RA   Griffiths S.A., Olson M.A., de Wit P.J., Bradshaw R.E.;
RT   "Dothistromin genes at multiple separate loci are regulated by AflR.";
RL   Fungal Genet. Biol. 51:12-20(2013).
RN   [7]
RP   FUNCTION.
RX   PubMed=23448391; DOI=10.1111/nph.12161;
RA   Bradshaw R.E., Slot J.C., Moore G.G., Chettri P., de Wit P.J.,
RA   Ehrlich K.C., Ganley A.R., Olson M.A., Rokas A., Carbone I., Cox M.P.;
RT   "Fragmentation of an aflatoxin-like gene cluster in a forest pathogen.";
RL   New Phytol. 198:525-535(2013).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the fragmented gene
CC       cluster that mediates the biosynthesis of dothistromin (DOTH), a
CC       polyketide toxin very similar in structure to the aflatoxin precursor,
CC       versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571,
CC       PubMed:23207690, PubMed:23448391). The first step of the pathway is the
CC       conversion of acetate to norsolorinic acid (NOR) and requires the fatty
CC       acid synthase subunits hexA and hexB, as well as the polyketide
CC       synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a
CC       hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize
CC       the precursor NOR (By similarity). The hexanoyl starter unit is
CC       provided to the acyl-carrier protein (ACP) domain by the fungal fatty
CC       acid synthase hexA/hexB (By similarity). The second step is the
CC       conversion of NOR to averantin (AVN) and requires the norsolorinic acid
CC       ketoreductase nor1, which catalyzes the dehydration of norsolorinic
CC       acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450
CC       monooxygenase avnA then catalyzes the hydroxylation of AVN to
CC       5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed
CC       by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690).
CC       Averufin might then be converted to hydroxyversicolorone by cypX and
CC       avfA (PubMed:23207690). Hydroxyversicolorone is further converted
CC       versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is
CC       then the substrate for the versiconal hemiacetal acetate esterase est1
CC       to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase
CC       vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC       ring (PubMed:16649078, PubMed:23207690). Then, the activity of the
CC       versicolorin B desaturase verB leads to versicolorin A (VERA)
CC       (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform
CC       epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a
CC       cytochrome P450, such as cypX or avnA could catalyze this step
CC       (PubMed:23207690). It is also possible that another, uncharacterized,
CC       cytochrome P450 enzyme is responsible for this step (PubMed:23207690).
CC       Opening of the epoxide could potentially be achieved by the epoxide
CC       hydrolase epoA (PubMed:23207690). However, epoA seems not to be
CC       required for DOTH biosynthesis, but other epoxide hydrolases may have
CC       the ability to complement this hydrolysis (PubMed:23207690).
CC       Alternatively, opening of the epoxide ring could be achieved non-
CC       enzymatically (PubMed:23207690). The next step is the deoxygenation of
CC       ring A to yield the 5,8-dihydroxyanthraquinone which is most likely
CC       catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690).
CC       The last stages of DOTH biosynthesis are proposed to involve
CC       hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might
CC       have oxidative roles here (PubMed:23207690). An alternative possibility
CC       is that cytochrome P450 monoogenases such as avnA and cypX might
CC       perform these steps in addition to previously proposed steps
CC       (PubMed:23207690). {ECO:0000250|UniProtKB:Q6UEF4,
CC       ECO:0000269|PubMed:12039746, ECO:0000269|PubMed:16649078,
CC       ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:17683963,
CC       ECO:0000305|PubMed:23207690, ECO:0000305|PubMed:23448391}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000303|PubMed:22069571,
CC       ECO:0000305|PubMed:23207690}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is positively regulated by the dothistromin-
CC       specific transcription factor aflR (PubMed:23207690). Dothistromin
CC       biosynthetic proteins are co-regulated, showing a high level of
CC       expression at ealy exponential phase with a subsequent decline in older
CC       cultures (PubMed:17683963). {ECO:0000269|PubMed:17683963,
CC       ECO:0000269|PubMed:23207690}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; DQ149246; AAZ95016.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q30DW6; -.
DR   SMR; Q30DW6; -.
DR   OMA; WTLMANE; -.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..511
FT                   /note="Cytochrome P450 monooxygenase cypX"
FT                   /id="PRO_0000443461"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         454
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        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   511 AA;  56700 MW;  0E273A0F34D277E0 CRC64;
     MAGELYKWIM DATAGAPLPF SLALVAAAFV LYNIVSIITT AYFSPLSKIP GPWYAKLTDL
     RLTYSVFAGN RIYYVDSLHQ KYGPMVRIGP KEVDVADPAA AREVHRMGTV FTKAPFYRLL
     SPGPVDNIFN FRDQKKHSQR RKLYAKGFTL VELRKNWEST INKTISMAVQ KMKEEAANGD
     TELMGWWTLM ANEIVCRLTF NGGHGTVEKG IKDPFVLMLE KRKGDLAHLL KMFIPPLYYV
     GRVLGKVNTR MNDIFYSQEK MFKAGAGVVK SARQDKEAGE FNQNLFAKAL QEGEGDAATL
     TDTDIITDAG ALLLAGSDPT AISLTFLIYL VLSRPELQKQ LEEEVASIDG EVTDTVCEGL
     PLMNAIIDES MRLYGAAPGG LPRSPPAGGA NLGGYYIPEG TVVDTQNWTL HTDGATWKEA
     QTFDHTRFLP ENRLEFSEKQ KMAFNPFGQG SRQCLGIHLG RLEMRLAVAH FFRELRGVKL
     AKSATPESMA VVDSFVAGVP RDRRCEVTMK A
 
 
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