PKFE_EMENI
ID PKFE_EMENI Reviewed; 309 AA.
AC Q5B8A2; A0A1U8QK97; C8VI78;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Prenyltransferase pkfE {ECO:0000303|PubMed:23706169};
DE EC=2.5.1.- {ECO:0000305|PubMed:23706169};
DE AltName: Full=Aspernidine A biosynthesis cluster protein pkfE {ECO:0000303|PubMed:23706169};
GN Name=pkfkE {ECO:0000303|PubMed:23706169}; ORFNames=ANIA_03228;
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, AND 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: Prenyltransferase; part of the gene cluster that mediates the
CC 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32378};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23706169}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of Aspernidine A.
CC {ECO:0000269|PubMed:23706169}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AACD01000054; EAA63129.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83143.1; -; Genomic_DNA.
DR RefSeq; XP_660832.1; XM_655740.1.
DR AlphaFoldDB; Q5B8A2; -.
DR SMR; Q5B8A2; -.
DR STRING; 162425.CADANIAP00009834; -.
DR EnsemblFungi; CBF83143; CBF83143; ANIA_03228.
DR EnsemblFungi; EAA63129; EAA63129; AN3228.2.
DR GeneID; 2874276; -.
DR KEGG; ani:AN3228.2; -.
DR eggNOG; KOG1381; Eukaryota.
DR HOGENOM; CLU_034879_2_0_1; -.
DR InParanoid; Q5B8A2; -.
DR OMA; TTTHYIN; -.
DR OrthoDB; 1343847at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="Prenyltransferase pkfE"
FT /evidence="ECO:0000255"
FT /id="PRO_0000446362"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 309 AA; 33432 MW; 9635B97B430EC6E3 CRC64;
MYSKSWILNA LPAPLVPYCE LTRVGYLPIG VLVSYLPVLV AILHVAAVAR LPYDNILDSC
LQWLPLCYVY SAYGCVVDDI ADQDLDRKVE RCQHRPLVRG AVSTTSACLF AASLASLAVF
LTKTFFPDQP AVHIPVALAG SIIYPFLKRF TNFALLYLAF LYVATGLNAS RTIGYDILSA
PDHLLTSNLL LAAAVFIANV SVETIYMHAD LEDDIKSGIG SLAVKIQGYS KPVLFLAAVA
YGSLVLASGL AAEFGKWYFT GAITSALTLF TLVARVDLKN GKMCEQFFFM GNAVLMSLLA
AGLYGECIA
