SDGD_EMENI
ID SDGD_EMENI Reviewed; 351 AA.
AC A0A1U8QW16; C8VPE3; Q5BCE5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Terpene cyclase sdgD {ECO:0000250|UniProtKB:A0A455R4Z0};
DE EC=5.4.99.- {ECO:0000269|PubMed:30302871};
DE AltName: Full=Aspernidgulenes biosynthesis cluster protein D {ECO:0000303|PubMed:30302871};
GN Name=sdgD {ECO:0000303|PubMed:30302871}; ORFNames=AN1785, ANIA_01785;
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, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=30302871; DOI=10.1002/cbic.201800486;
RA Lin T.S., Chen B., Chiang Y.M., Wang C.C.C.;
RT "Discovery and elucidation of the biosynthesis of aspernidgulenes: novel
RT polyenes from Aspergillus nidulans by using serial promoter replacement.";
RL ChemBioChem 20:329-334(2019).
CC -!- FUNCTION: Epoxide hydrolase; part of the gene cluster that mediates the
CC biosynthesis of the polyenes aspernidgulenes (PubMed:30302871). The
CC carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA,
CC which accepts acetyl-CoA as the starter unit and performs malonyl-CoA
CC extensions as well as regioselective methylation and reduction
CC (PubMed:30302871). The resulting nonaketide offloads the HR-PKS by
CC intramolecular lactonization to yield the 5,6-dihydro-alpha-pyrone-
CC containing hexaenoic acids preaspernidgulene A1 and A2
CC (PubMed:30302871). The FAD-dependent monooxygenase sdgC then installs
CC the first epoxide on the penultimate double bond (PubMed:30302871).
CC Subsequently, the FAD-dependent monooxygenase sdgF presumably generates
CC a ketone intermediate through Meinwald rearrangement involving a
CC hydride shift (PubMed:30302871). Next, sdgC introduces another epoxide
CC on the last olefin of the ketone intermediate after E/Z isomerization
CC (PubMed:30302871). The epoxide hydrolase sdgD then catalyzes
CC stereospecific cyclization of the 5,6-dihydro-alpha-pyrone and opening
CC of the epoxide ring to form an oxygenated trimethylcyclopentanone and
CC an oxabicyclo[2.2.1]heptane unit (PubMed:30302871). Finally, the
CC bicyclic unit undergoes hydrolytic cleavage, either spontaneously or
CC catalyzed by sdgD, to assemble the dimethyl-gamma-lactone moiety in
CC aspernidgulene A1 (PubMed:30302871). {ECO:0000269|PubMed:30302871}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30302871}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family.
CC {ECO:0000305}.
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DR EMBL; BN001307; CBF85557.1; -; Genomic_DNA.
DR EMBL; AACD01000028; EAA63961.1; -; Genomic_DNA.
DR RefSeq; XP_659389.1; XM_654297.1.
DR AlphaFoldDB; A0A1U8QW16; -.
DR EnsemblFungi; CBF85557; CBF85557; ANIA_01785.
DR EnsemblFungi; EAA63961; EAA63961; AN1785.2.
DR GeneID; 2875013; -.
DR KEGG; ani:AN1785.2; -.
DR VEuPathDB; FungiDB:AN1785; -.
DR eggNOG; ENOG502SHVK; Eukaryota.
DR HOGENOM; CLU_038717_0_0_1; -.
DR OMA; ERDEMVF; -.
DR OrthoDB; 1036136at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Isomerase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..351
FT /note="Terpene cyclase sdgD"
FT /id="PRO_0000451914"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 351 AA; 39043 MW; BAAA58B39D7236CB CRC64;
MSHQSTINFI RFTFVILSLL AIYTILIPSI RKGFFQHITE CEVTGKLSRS SGADARMIES
FTGVPVLDIF VKALVTSFWP VINGENPALS LLGVPAVASM GVSYLLLLLE ARRTRSLLSV
TWRLAWVGLL QTNFSQAIIL PIYCAIAFSS SKKTNGFRPI PHVTISLILC VYTGMALVAL
PSPAVIPDGL KQVVVAFMVP WALWVFVMVF MASYLFPIEV EKEKSRRTIY IFALVIAATT
HLGALLASLL HADLGPADVF LPPLPWYVTR FPSLEEGMAS FLQWDYLIAS VTLFLWAVAV
YLRDCDEHVD WQRFGLEVCA ISVIISPAAM AVLLIWRLDE MLSRRGIAKE D
