PBCA_EMENI
ID PBCA_EMENI Reviewed; 979 AA.
AC A0A1U8QHE3; C8VN87; Q5BCY6;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Pimaradiene synthase pbcA {ECO:0000303|PubMed:22506079};
DE EC=4.2.3.- {ECO:0000305|PubMed:22506079};
DE EC=5.5.1.- {ECO:0000305|PubMed:22506079};
DE AltName: Full=Bifunctional terpene synthase pbcA {ECO:0000303|PubMed:22506079};
DE AltName: Full=Pimaradiene biosynthesis cluster protein A {ECO:0000303|PubMed:22506079};
GN Name=pbcA {ECO:0000303|PubMed:27098256}; ORFNames=AN1594, ANIA_01594;
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, INDUCTION, DOMAIN, AND PATHWAY.
RX PubMed=22506079; DOI=10.1371/journal.pone.0035450;
RA Bromann K., Toivari M., Viljanen K., Vuoristo A., Ruohonen L.,
RA Nakari-Setaelae T.;
RT "Identification and characterization of a novel diterpene gene cluster in
RT Aspergillus nidulans.";
RL PLoS ONE 7:e35450-e35450(2012).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27098256; DOI=10.1007/s00253-016-7517-5;
RA Bromann K., Toivari M., Viljanen K., Ruohonen L., Nakari-Setaelae T.;
RT "Engineering Aspergillus nidulans for heterologous ent-kaurene and gamma-
RT terpinene production.";
RL Appl. Microbiol. Biotechnol. 100:6345-6359(2016).
CC -!- FUNCTION: Bifunctional terpene synthase; part of the gene cluster that
CC mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene
CC (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-
CC CoA reductase AN1593 functions in the mevalonate pathway, which
CC produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The
CC geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the
CC formation of GGPP, the precursor for diterpenes (PubMed:22506079,
CC PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2
CC cyclization steps that convert GGPP to ent-pimara-8(14),15-diene
CC (PubMed:22506079, PubMed:27098256). The putative roles of the remaining
CC cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear
CC (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione
CC S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably
CC function as decorative enzymes (Probable). It is possible that in
CC biological conditions the compound is oxidized to ent-pimara-8(14),15-
CC dien-19-oic acid, which is a bioactive diterpene compound predominant
CC in many plant extracts (Probable). {ECO:0000269|PubMed:22506079,
CC ECO:0000269|PubMed:27098256, ECO:0000305|PubMed:22506079}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:27098256}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pbcR. {ECO:0000269|PubMed:22506079,
CC ECO:0000269|PubMed:27098256}.
CC -!- DOMAIN: The VYDTAW motif is widely conserved among diterpene cyclases
CC in plants and fungi. {ECO:0000305|PubMed:22506079}.
CC -!- DOMAIN: The DXDD B-type cyclization motif at positions 328-331 is
CC responsible for the formation of ent-CDP.
CC {ECO:0000305|PubMed:22506079}.
CC -!- DOMAIN: The DEXXE A-type cyclization motif at positions 664-668 is
CC responsible for the formation of ent-kaurene.
CC {ECO:0000305|PubMed:22506079}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ent-pimara-8(14),15-
CC diene (PD). {ECO:0000269|PubMed:27098256}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AACD01000025; EAA64301.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85181.1; -; Genomic_DNA.
DR RefSeq; XP_659198.1; XM_654106.1.
DR AlphaFoldDB; A0A1U8QHE3; -.
DR SMR; A0A1U8QHE3; -.
DR EnsemblFungi; CBF85181; CBF85181; ANIA_01594.
DR EnsemblFungi; EAA64301; EAA64301; AN1594.2.
DR GeneID; 2875701; -.
DR KEGG; ani:AN1594.2; -.
DR eggNOG; ENOG502QUXU; Eukaryota.
DR HOGENOM; CLU_005861_0_0_1; -.
DR OMA; CRMYNDY; -.
DR OrthoDB; 372122at2759; -.
DR BRENDA; 4.2.3.30; 517.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR017057; Ent-kaurene_synthase_fun.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PIRSF; PIRSF036498; Ent-kaurene_synthase_fungi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..979
FT /note="Pimaradiene synthase pbcA"
FT /id="PRO_0000450839"
FT MOTIF 34..39
FT /note="VYDTAW motif"
FT /evidence="ECO:0000305|PubMed:22506079"
FT MOTIF 328..331
FT /note="DXDD B-type cyclization motif"
FT /evidence="ECO:0000305|PubMed:22506079"
FT MOTIF 664..668
FT /note="DEXXE A-type cyclization motif"
FT /evidence="ECO:0000305|PubMed:22506079"
SQ SEQUENCE 979 AA; 110118 MW; E7FDB85F172CD36D CRC64;
MTCADVTDLC TQASQLVQQL RTKDGELGFM SAAVYDTAWV SMVQKTTPEG RQWLLPKCFE
YILRTQLEDG SWETYASDVD GILNTAASLL ALETHAESRI ASTDPPVEEM KERIGRARAA
LSRQLQAWSV KDTVHVGFEI ILPALLRLLR EKGHEFEFDG RAELDRLNRI KLSKFRPEYL
YSARTTALHS LEAFVGMIDF DKVAHQKVNG SFMFSPSSTA AFLMFSSSWD DECEQYLRLV
LQNGAGGGTG GMPSAYPSKY FEVSWVRGQL ARLESKLTEL QALTTLLDNG YSTGDLGIED
TDSLGEMLRD ALVKGGGIVG FAPSIQADAD DTAKSLIAVS LLDKPVSAQG LIDAFEGPMH
FRTYHGERDP SFTANSNVLL ALLNTPDAAT VSPQIEKAAA FLCDVWWTAD SEIGDKWNLS
PYYPSMLMAE AFGKLLQVWS DGGLKSISSQ FIRDRVSVCL YQALVRTLQT QNENGSWGSH
SHEETAYAIL TIAHACQLPV VNQLWTNVQL AVSRGRKFLQ NSAGDKAEYL WVEKVTYSSI
LLSKSYVLAA LKVSFERSYP ACLANLFIVS KKRVIEFARF HSMLPLFSSM ELWKVRAAIV
EGYLLLPQLR DRRLAVFSRT GMEEDKYFEY IPFTWTLCNN RRNTFLSTKT LVEMMVISFL
NYQADEFMEA VVGRLNSSQR SMTRSCIDEI FRDLKDKPEL NDAIQAQSGP RNADANGHRI
LPQAKRIKMG SQLPSDVSRV LSAFVHHVMD HPSVKAAAPL EYERVKNELQ VFLLSHIEQA
DDNGRFAAQL ESTRDDFETA RSSFYRWVSS TSSDHTSCPY SFAFYQCLLG FEQASHNAAC
FQTCEEKYVA EAMCRHLAVM CRMYNDYGSL ARDRDEKNLN CVNFPEFAQA GPKSDAVRQK
QLFSLAEFER SNMKRGLEVL TEMAAQDRAK MRMLEKVQMF CDVTDVYGQI YALEILRVGC
DLAHDCFMLE LPAQWSNST
