ID   ALNG_EMENI              Reviewed;         368 AA.
AC   P0CU77; A0A1U8QXS7; C8VJR1; Q5AR59;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Terpene cyclase alnG {ECO:0000250|UniProtKB:A0A455R4Z0};
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:A0A455R4Z0};
DE   AltName: Full=Asperlin biosynthesis cluster protein G {ECO:0000303|PubMed:30339758};
GN   Name=alnG {ECO:0000303|PubMed:30339758}; ORFNames=AN9221;
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   GENE MODEL REVISION, IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION,
RP   INDUCTION, AND PATHWAY.
RX   PubMed=30339758; DOI=10.1021/acschembio.8b00679;
RA   Grau M.F., Entwistle R., Chiang Y.M., Ahuja M., Oakley C.E., Akashi T.,
RA   Wang C.C.C., Todd R.B., Oakley B.R.;
RT   "Hybrid transcription factor engineering activates the silent secondary
RT   metabolite gene cluster for (+)-asperlin in Aspergillus nidulans.";
RL   ACS Chem. Biol. 13:3193-3205(2018).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       asperlin, a polyketide showing anti-inflammatory, antitumor and
CC       antibiotic activities (PubMed:30339758). The first step of the asperlin
CC       biosynthesis is the production of the intermediate 2,4,6-octatrienoic
CC       acid by the highly redusing polyketide synthase alnA with cleavage of
CC       the PKS product by the esterase alnB (PubMed:30339758). 2,4,6-
CC       octatrienoic acid is further converted to asperlin via several steps
CC       involving the remaining enzymes from the cluster (PubMed:30339758).
CC       {ECO:0000269|PubMed:30339758}.
CC   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is controlled by the asperlin biosynthesis
CC       cluster-specific transcription factor alnR.
CC       {ECO:0000269|PubMed:30339758}.
CC   -!- DISRUPTION PHENOTYPE: Strongly diminishes the production of asperlin.
CC       {ECO:0000269|PubMed:30339758}.
CC   -!- SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF82293.1; Type=Erroneous gene model prediction; Note=The predicted gene AN9221 has been split into 2 genes: alnG and alnR.; Evidence={ECO:0000305|PubMed:30339758};
CC       Sequence=EAA61512.1; Type=Erroneous gene model prediction; Note=The predicted gene AN9221 has been split into 2 genes: alnG and alnR.; Evidence={ECO:0000305|PubMed:30339758};
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DR   EMBL; AACD01000170; EAA61512.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF82293.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0CU77; -.
DR   EnsemblFungi; CBF82293; CBF82293; ANIA_09221.
DR   EnsemblFungi; EAA61512; EAA61512; AN9221.2.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Isomerase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..368
FT                   /note="Terpene cyclase alnG"
FT                   /id="PRO_0000445950"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   368 AA;  40735 MW;  CBE23AC8F61B45EF CRC64;
     MTRQIPLLAL SWLELIFFSC YYGGLAGLGY HSLWRIALRR RNVAPAIKSV LQTGRFADGT
     PLTRRYTNLE FLDKKLVPAV IFYDGLLTGA CPLYRLLLVD IHSTMQAMAL CMLVSTRSKS
     LSTISLLLPT FWNVFNQFYG AAFVYPLYLL LEAVTTGFNP LYPVETETSR SALLVSAMIG
     SFLPFTFLWP AFLRSGTESR QRAIALYRFA PVVFSLLQIV GEKVLGAQMI PQPTSQASPY
     LVAGCAATVG HWYALGGALG LAMRLSHRKG RLGALTLVLK RLYLPRSAEE TTRLDASVLA
     RAAHEFLQYD VLVLIAAYIP YAYYLLAPLN LASPFAMVVS LVLGTIFLGP GAVLAFAYRV
     RWHLAISD