PHMB_PHANO
ID PHMB_PHANO Reviewed; 598 AA.
AC Q0V6Q8;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Cytochrome P450 monooxygenase phmB {ECO:0000303|PubMed:31815421};
DE EC=1.-.-.- {ECO:0000305|PubMed:31815421};
DE AltName: Full=Phomacin biosynthesis cluster protein B {ECO:0000303|PubMed:31815421};
GN Name=phmB {ECO:0000303|PubMed:31815421}; ORFNames=SNOG_00306;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=31815421; DOI=10.1021/acschembio.9b00791;
RA Li H., Wei H., Hu J., Lacey E., Sobolev A.N., Stubbs K.A., Solomon P.S.,
RA Chooi Y.H.;
RT "Genomics-driven discovery of phytotoxic cytochalasans involved in the
RT virulence of the wheat pathogen Parastagonospora nodorum.";
RL ACS Chem. Biol. 15:226-233(2020).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxins phomacins, leucine-derived
CC cytochalasans with potent actin polymerization-inhibitory activities
CC and monocot-specific antigerminative activities (PubMed:31815421). The
CC first step in the pathway is catalyzed by the hybrid PKS-NRPS phmA,
CC assisted by the enoyl reductase phmE, that are responsible for fusion
CC of the leucine precursor and the polyketide backbone to produce a 2-
CC pyrrolidone intermediate (PubMed:31815421). The polyketide synthase
CC module (PKS) of phmA is responsible for the synthesis of the polyketide
CC backbone and the downstream nonribosomal peptide synthetase (NRPS)
CC amidates the carboxyl end of the polyketide with the leucine precursor
CC (PubMed:31815421). Because phmA lacks a designated enoylreductase (ER)
CC domain, the required activity is provided the enoyl reductase phmE
CC (PubMed:31815421). Reduction by the hydrolyase phmG, followed by
CC dehydration and intra-molecular Diels-Alder cyclization by the Diels-
CC Alderase phmD then yield the required isoindolone-fused macrocycle
CC (Probable). A number of oxidative steps catalyzed by the tailoring
CC cytochrome P450 monooxygenase phmB, the FAD-linked oxidoreductase phmC
CC and the short-chain dehydrogenase/reductase phmF, are further required
CC to afford the final products, phomacin D and phomacin E
CC (PubMed:31815421). {ECO:0000269|PubMed:31815421,
CC ECO:0000305|PubMed:31815421}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:31815421}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CH445325; EAT91801.1; -; Genomic_DNA.
DR RefSeq; XP_001790996.1; XM_001790944.1.
DR AlphaFoldDB; Q0V6Q8; -.
DR SMR; Q0V6Q8; -.
DR EnsemblFungi; SNOT_00306; SNOT_00306; SNOG_00306.
DR GeneID; 5968090; -.
DR KEGG; pno:SNOG_00306; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_022195_0_2_1; -.
DR InParanoid; Q0V6Q8; -.
DR OMA; KINACAF; -.
DR OrthoDB; 574756at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..598
FT /note="Cytochrome P450 monooxygenase phmB"
FT /id="PRO_0000449433"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 542
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 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 598 AA; 68056 MW; 44DC6ED326D74E15 CRC64;
MAFPGVRRGL GELIGLRKSD AWYSTEDPRF GLTCRITAST RKLASCTSPW QYADIIQFIA
STTITTIMLE SLIEQWQIMR QAFAPMRLSR WQLVKLLAAQ IHRDNPVAAK IAALLFVAGL
FWAVSVLTRP KRLDKKLGLP LIGGSRTLKK DFATVIERGR QMYPDQPFIV NSSGKPFVVY
PPSNFDEIKR LSEEEASAQD FFYDATHGYW TSVGTETPAL WKTIGIDLAR AGAPVVSTKQ
KDARTAFDRY VGYCPDEKSF NVFDVMMKVV ALTNGASFVG REVAGGRWHE LVAQLPMTVY
FAVIFLTWTP RLFRPFLEPL FFLPHFKVQR DMRRILEPII KQDLDEWSKT DDKKEQLKVK
EGQRLPYHKW LISRYGPGEA TPRQLATDQI VTAFESTIST ALTIYYILFQ LASRPELQDE
LRQEIADNTT DGQLPSTSLT ELRKMDSVMR ESFRVNPFAL FSLYRITRKP LQLSTGPKLP
AGTIFCVDVH HINNSSALFP APTRYDPHRF LNKREQPGAE HRHQFVSTGP MDPNFGDGTQ
ACPGRFWANN TIKVCLVHVL TRYRLKLKEG HTRPQPVCMP NGSWVPDLKA EVIFQSLD
