ALND_EMENI
ID ALND_EMENI Reviewed; 553 AA.
AC A0A1U8QFC3; C8VJR4; Q5AR62;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Cytochrome P450 monooxygenase alnD {ECO:0000303|PubMed:30339758};
DE EC=1.-.-.- {ECO:0000305|PubMed:30339758};
DE AltName: Full=Asperlin biosynthesis cluster protein D {ECO:0000303|PubMed:30339758};
GN Name=alnD {ECO:0000303|PubMed:30339758}; ORFNames=AN9218.2;
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 IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, 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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of asperlin, a polyketide showing anti-
CC inflammatory, antitumor and antibiotic activities (PubMed:30339758).
CC The first step of the asperlin biosynthesis is the production of the
CC intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide
CC synthase alnA with cleavage of the PKS product by the esterase alnB
CC (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to
CC asperlin via several steps involving the remaining enzymes from the
CC cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-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: Fully eliminates the production of asperlin.
CC {ECO:0000269|PubMed:30339758}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AACD01000170; EAA61509.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF82299.1; -; Genomic_DNA.
DR RefSeq; XP_682487.1; XM_677395.1.
DR AlphaFoldDB; A0A1U8QFC3; -.
DR SMR; A0A1U8QFC3; -.
DR EnsemblFungi; CBF82299; CBF82299; ANIA_09218.
DR EnsemblFungi; EAA61509; EAA61509; AN9218.2.
DR GeneID; 2867991; -.
DR KEGG; ani:AN9218.2; -.
DR VEuPathDB; FungiDB:AN9218; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_31_0_1; -.
DR OMA; PRYISLE; -.
DR OrthoDB; 1247045at2759; -.
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 Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..553
FT /note="Cytochrome P450 monooxygenase alnD"
FT /id="PRO_0000445942"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 493
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 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 553 AA; 62670 MW; 28D27D14ECA8B1EE CRC64;
MTVQTFYLIG EKERSTRELD VGDPKTVNAL RQGLAEVFNI LSAEGIDFHD CHGPISTIES
ILRSESVGIT VNGHPVRYPQ QPQGIPIFGN HFEIYPDHLG NHERLFNKYG SVIRTNNMGR
VTYLTNDPDI AALAFRDNDY FTKAPSSASH PLYGIRDQTA LFLCDTESPA WKEAHKFIPP
SMTPRAVRHY TPLLQQSVDT VFNVLDKFDN NGQAFNVYHL TAKLASQVIC QLVLGVDLHH
FDAVDSPVHP IIVLLQRYLT LNRRVQTKGA WYSYLPFGDP VALKNTRREL YGLIEEAVIT
CQKKNGGTTG DLPIQTAALH ATCLVDYLAR ATDEHGNKLR HEYILSNTLA LVGAGFVTSS
AFLSWLIYSL VEYPGQQDRL LQELVDHGAV SDKRWTYDEI QALPFLDAFV KEAQRMHSPS
FQPARNVKKD IILPGGWALP QGSILIPSIP HLHHHTAYWE NPDRFDPDRW RTEKVKNRHR
SVYVPFAAGP RSCIGFNVAL QEVKISLAEL VYRYEFVNAT NEGIEYDPDF IVIRPVNFYV
RAIRRTEWPA RSP
