ORSC_EMENI
ID ORSC_EMENI Reviewed; 369 AA.
AC Q5AUW8; C8V4V2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Tyrosinase-like protein orsC {ECO:0000303|PubMed:20174687};
DE EC=1.14.-.- {ECO:0000305|PubMed:20174687};
DE AltName: Full=Orsellinic acid/F9775 biosynthesis cluster protein C {ECO:0000303|PubMed:19666480};
DE Flags: Precursor;
GN Name=orsC {ECO:0000303|PubMed:19666480}; ORFNames=AN7912;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
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: Tyrosinase-like protein; part of the gene cluster that
CC mediates the biosynthesis of orsellinic acid, as well as of the
CC cathepsin K inhibitors F9775 A and F9775 B (PubMed:19666480,
CC PubMed:20174687). The non-reducing polyketide synthase orsA produces
CC orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units
CC (PubMed:19666480, PubMed:20174687). Further modifications by the
CC decarboxylase orsB and the tyrosinase-like protein orsC lead to the
CC production of F9775 A and F9775 B (PubMed:20174687). The functions of
CC orsD and orsE remain unclear since only orsB and orsC are required to
CC convert orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
CC {ECO:0000269|PubMed:19666480, ECO:0000269|PubMed:20174687}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20174687}.
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 -!- DISRUPTION PHENOTYPE: Fails to produce F9775 A and B, but accumulates
CC diorcinol and continues to yield orsellinic acid (PubMed:20174687).
CC {ECO:0000269|PubMed:20174687}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001302; CBF73509.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59566.1; -; Genomic_DNA.
DR RefSeq; XP_681181.1; XM_676089.1.
DR AlphaFoldDB; Q5AUW8; -.
DR SMR; Q5AUW8; -.
DR STRING; 162425.CADANIAP00003930; -.
DR EnsemblFungi; CBF73509; CBF73509; ANIA_07912.
DR EnsemblFungi; EAA59566; EAA59566; AN7912.2.
DR GeneID; 2869303; -.
DR KEGG; ani:AN7912.2; -.
DR eggNOG; ENOG502RM4B; Eukaryota.
DR HOGENOM; CLU_035914_0_1_1; -.
DR InParanoid; Q5AUW8; -.
DR OMA; FHHAQVD; -.
DR OrthoDB; 518234at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
KW Copper; Glycoprotein; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..369
FT /note="Tyrosinase-like protein orsC"
FT /evidence="ECO:0000255"
FT /id="PRO_5007924264"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P06845"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P06845"
FT BINDING 315
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P06845"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 369 AA; 41912 MW; 17FA3D7508963481 CRC64;
MLAFNPLVTA LAALIFLFCQ ANANPPLMQR LVHEYQWKTK QGLPRQGACT PHNLAVRREW
STLDVETRLE YIEAVKCLAR LPSIIDPELA PGARSRFDDF QATHIRHTRT IHATGSFFAW
HRHFVYLYEK ALREECGYTG YQPYWEWSHW ANLPITANPL YDGSNASLSG NGVYIPNRNG
TLQLFPIPNP SPDTAIYTPP GTGGGYIYDG PLVDWELHLG PVLYSYDNGQ YIPPNPRPDG
LGYNPRPLIR DFNNTLLQQG ASWDIILNML VNVTDMHEFH PLFFQGPHLA GHIFISGVDN
DIFTSPGDPL FWFHHAQVDR IWTIWQALDL ETREYALDGT LTLLNCKNLP FRRILAGELT
VCDDSTAQP
