PKFB_EMENI
ID PKFB_EMENI Reviewed; 508 AA.
AC C8VI81; Q5B8A5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cytochrome P450 monooxygenase pkfB {ECO:0000303|PubMed:23706169};
DE EC=1.-.-.- {ECO:0000269|PubMed:23706169};
DE AltName: Full=Aspernidine A biosynthesis cluster protein pkfB {ECO:0000303|PubMed:23706169};
GN Name=pkfkB {ECO:0000303|PubMed:23706169}; ORFNames=ANIA_03225;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RX PubMed=22510154; DOI=10.1021/ja3016395;
RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT nidulans.";
RL J. Am. Chem. Soc. 134:8212-8221(2012).
RN [4]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=23706169; DOI=10.1021/ol401187b;
RA Yaegashi J., Praseuth M.B., Tyan S.W., Sanchez J.F., Entwistle R.,
RA Chiang Y.M., Oakley B.R., Wang C.C.;
RT "Molecular genetic characterization of the biosynthesis cluster of a
RT prenylated isoindolinone alkaloid aspernidine A in Aspergillus nidulans.";
RL Org. Lett. 15:2862-2865(2013).
RN [5]
RP INDUCTION.
RX PubMed=25701285; DOI=10.1534/genetics.115.174342;
RA Oiartzabal-Arano E., Garzia A., Gorostidi A., Ugalde U., Espeso E.A.,
RA Etxebeste O.;
RT "Beyond asexual development: modifications in the gene expression profile
RT caused by the absence of the Aspergillus nidulans transcription factor
RT FlbB.";
RL Genetics 199:1127-1142(2015).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of aspernidine A, a prenylated isoindolinone
CC (PubMed:23706169). The starting point of the biosynthesis of aspernidin
CC A is the production of orsellinaldehyde by the non-reducing polyketide
CC synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of
CC the phenol groups, and prenylation, presumably catalyzed by the
CC prenyltransferase pkfE, would be needed to yield aspernidine D
CC (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is
CC responsible for hydroxylation of aspernidine D to yield aspernidine E
CC (PubMed:23706169). The dehydrogenase pkfF may be responsible for
CC further oxidation of aspernidine E to form a dialdehyde intermediate
CC which is further transformed in a series of steps, some of which are
CC enzyme-mediated, to generate aspernidine A (Probable). The possibility
CC that additional enzymes outside of the cluster are involved in
CC aspernidine A biosynthesis cannot be excluded (Probable).
CC {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:23706169,
CC ECO:0000305|PubMed:23706169}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23706169}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of aspernidine A, but
CC accumulates the intermediate aspernidine D.
CC {ECO:0000269|PubMed:23706169}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA63126.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000054; EAA63126.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF83149.1; -; Genomic_DNA.
DR RefSeq; XP_660829.1; XM_655737.1.
DR AlphaFoldDB; C8VI81; -.
DR SMR; C8VI81; -.
DR EnsemblFungi; CBF83149; CBF83149; ANIA_03225.
DR EnsemblFungi; EAA63126; EAA63126; AN3225.2.
DR GeneID; 2874149; -.
DR KEGG; ani:AN3225.2; -.
DR VEuPathDB; FungiDB:AN3225; -.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR InParanoid; C8VI81; -.
DR OMA; MPYTRKG; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; 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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..508
FT /note="Cytochrome P450 monooxygenase pkfB"
FT /id="PRO_0000446360"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
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 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 508 AA; 57688 MW; A5EB641DD6E9CED6 CRC64;
MDHPHPSTFS LGLSQILVCL ALLYAAIHIL SVYRRLCHIS GPFWARISNL PRVWWVNTSR
AHEIHQQLHE KYGDVVRFGP NMVSLRNPTW IPTVYPTRMG VKKSDFYRTL APYTPSGALP
AVFSSRDEEV HRGLRGPIAS LYSMSKVLPL EVFVDRTIDV LVRQLDGRFA GAGETFDLAS
WLQFFAFDVM GTLTFSKRYG FLEKGMDVHG MLDTIWRFLK GAAPFTQIPW VDEIWNKNVL
ATKLKGATGV SILGIVGKFV SQRQEESKAG KIDGTADRDM LSLFMEIQKN NQLPPWYVTA
WTFSNITAGS DSAAVVMRTV FYNLLSHPST LQKLRSELLS AGPLTQPYPS WKDVCNLPYL
DACILEALRL HPPFCLPFER IVPQGGMVLG DTYFPEGTVV GMSPWVVNRH KPTFGEDSDV
WNPERWMVSK ELKSKREAAV LTFGAGRRVC LGRHIAILEL KKIVPALVLR YDFELIDPER
FTTENFWFFR QRGMDVRVKK RMQAEAGI
