ORSE_EMENI
ID ORSE_EMENI Reviewed; 348 AA.
AC Q5AUW6; C8V4V4;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Dehydrogenase orsE {ECO:0000303|PubMed:23841751};
DE EC=1.-.-.- {ECO:0000305};
DE AltName: Full=Enoyl reductase orsE {ECO:0000305};
DE AltName: Full=Orsellinic acid/F9775 biosynthesis cluster protein E {ECO:0000303|PubMed:19666480};
GN Name=orsE {ECO:0000303|PubMed:19666480}; ORFNames=AN7914;
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 OF THE ORS CLUSTER, FUNCTION, AND INDUCTION.
RX PubMed=19666480; DOI=10.1073/pnas.0901870106;
RA Schroeckh V., Scherlach K., Nuetzmann H.W., Shelest E., Schmidt-Heck W.,
RA Schuemann J., Martin K., Hertweck C., Brakhage A.A.;
RT "Intimate bacterial-fungal interaction triggers biosynthesis of archetypal
RT polyketides in Aspergillus nidulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14558-14563(2009).
RN [4]
RP FUNCTION.
RX PubMed=20174687; DOI=10.1039/b904541d;
RA Sanchez J.F., Chiang Y.M., Szewczyk E., Davidson A.D., Ahuja M.,
RA Elizabeth Oakley C., Woo Bok J., Keller N., Oakley B.R., Wang C.C.;
RT "Molecular genetic analysis of the orsellinic acid/F9775 gene cluster of
RT Aspergillus nidulans.";
RL Mol. Biosyst. 6:587-593(2010).
RN [5]
RP INDUCTION.
RX PubMed=23892751; DOI=10.1128/aem.01578-13;
RA Nuetzmann H.W., Fischer J., Scherlach K., Hertweck C., Brakhage A.A.;
RT "Distinct amino acids of histone H3 control secondary metabolism in
RT Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 79:6102-6109(2013).
RN [6]
RP INDUCTION.
RX PubMed=23841751; DOI=10.1111/mmi.12326;
RA Bok J.W., Soukup A.A., Chadwick E., Chiang Y.M., Wang C.C., Keller N.P.;
RT "VeA and MvlA repression of the cryptic orsellinic acid gene cluster in
RT Aspergillus nidulans involves histone 3 acetylation.";
RL Mol. Microbiol. 89:963-974(2013).
CC -!- FUNCTION: Dehydrogenase; part of the gene cluster that mediates the
CC biosynthesis of orsellinic acid, as well as of the cathepsin K
CC inhibitors F9775 A and F9775 B (PubMed:19666480, PubMed:20174687). The
CC non-reducing polyketide synthase orsA produces orsellinic acid by
CC condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:19666480,
CC PubMed:20174687). Further modifications by the decarboxylase orsB and
CC the tyrosinase-like protein orsC lead to the production of F9775 A and
CC F9775 B (PubMed:20174687). The functions of orsD and orsE remain
CC unclear since only orsB and orsC are required to convert orsellinic
CC acid into F9775 A and F9775 B (PubMed:20174687).
CC {ECO:0000269|PubMed:19666480, ECO:0000269|PubMed:20174687}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC -!- INDUCTION: Expression is induced by an intimate physical interaction of
CC the fungal mycelia with the bacterium Streptomyces hygroscopicus
CC (PubMed:19666480). Expression is repressed by VeA and MvlA via histone
CC 3 acetylation by the SAGA/ADA complex (PubMed:23892751,
CC PubMed:23841751). {ECO:0000269|PubMed:19666480,
CC ECO:0000269|PubMed:23841751, ECO:0000269|PubMed:23892751}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; BN001302; CBF73513.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59568.1; -; Genomic_DNA.
DR RefSeq; XP_681183.1; XM_676091.1.
DR AlphaFoldDB; Q5AUW6; -.
DR SMR; Q5AUW6; -.
DR STRING; 162425.CADANIAP00003932; -.
DR EnsemblFungi; CBF73513; CBF73513; ANIA_07914.
DR EnsemblFungi; EAA59568; EAA59568; AN7914.2.
DR GeneID; 2869245; -.
DR KEGG; ani:AN7914.2; -.
DR VEuPathDB; FungiDB:AN7914; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_16_5_1; -.
DR InParanoid; Q5AUW6; -.
DR OMA; IQDYGIF; -.
DR OrthoDB; 727365at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IBA:GO_Central.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0019748; P:secondary metabolic process; IEP:AspGD.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..348
FT /note="Dehydrogenase orsE"
FT /id="PRO_0000438581"
FT BINDING 43..46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 130..137
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 180..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 203..206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 272..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 292..296
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 339..340
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 348 AA; 35972 MW; 2A7D7461EC0953A0 CRC64;
MATNQAAWLT KAGNDLEVGD APVPTAGPGE IVVKNAAVAI NPLDTHMQDV GVFVQQWPTI
FGCDVAGTVH ETGPDVERFK KGDRVIGHAI NLVTGRPQDG AYALYTVVPA NKAAILPDAI
SFTDGVVAPF AVEAAVCVLS LKEPGVAMPG VSTPALALPY PSLDDPVKPL GKVLVIWGGS
SSVGSMTTQI ATAAGIQVIA ISGAHNFELS KRCGATEVFD HKDPEVVDKV VAAVQKSGQE
FVGIFDAVAT PDTYTSDLVI LEKLGGGHLA AVHPPPAEVP SNVKAGMIFA VNDIATPVWN
DFVTPALESG KIQCLPPPTI VGKGLEAINE GLKRCKAGVS ATKLVVEL
