ORSB_EMENI
ID ORSB_EMENI Reviewed; 331 AA.
AC Q5AUW9; C8V4V1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Decarboxylase orsB {ECO:0000303|PubMed:20174687};
DE EC=4.1.1.- {ECO:0000305|PubMed:20174687};
DE AltName: Full=Orsellinic acid/F9775 biosynthesis cluster protein B {ECO:0000303|PubMed:19666480};
GN Name=orsB {ECO:0000303|PubMed:19666480}; ORFNames=AN7911;
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: Decarboxylase; 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 -!- 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 gerfelin and continues to yield orsellinic acid (PubMed:20174687).
CC {ECO:0000269|PubMed:20174687}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; BN001302; CBF73507.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59565.1; -; Genomic_DNA.
DR RefSeq; XP_681180.1; XM_676088.1.
DR AlphaFoldDB; Q5AUW9; -.
DR SMR; Q5AUW9; -.
DR STRING; 162425.CADANIAP00003929; -.
DR EnsemblFungi; CBF73507; CBF73507; ANIA_07911.
DR EnsemblFungi; EAA59565; EAA59565; AN7911.2.
DR GeneID; 2869268; -.
DR KEGG; ani:AN7911.2; -.
DR VEuPathDB; FungiDB:AN7911; -.
DR eggNOG; KOG4245; Eukaryota.
DR HOGENOM; CLU_039329_5_1_1; -.
DR InParanoid; Q5AUW9; -.
DR OMA; WHTETGL; -.
DR OrthoDB; 941496at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1900611; P:F-9775A biosynthetic process; IMP:AspGD.
DR GO; GO:1900614; P:F-9775B biosynthetic process; IMP:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; IEP:AspGD.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..331
FT /note="Decarboxylase orsB"
FT /id="PRO_0000438578"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
SQ SEQUENCE 331 AA; 36778 MW; 72A9F806EDF734F8 CRC64;
MTPPLLALEE HYYSTAIFNS IGETFQRTLQ GVPGLADQLR SLGDGRLEAM NRGNISLQVV
SHAFTPGGPS AEACRAGNDE LAAEIAQISD PQRFAAFAVL PVADPTASAA ELDRSVSELG
FVGALIDNHA DGKHFDGHDY DVLWAKACEL DVPIYLHPTW PSARMAENFM GSYPVPVGIS
LGGPGWGWHP DVGLHVLKLF AAGVFDRFPR LKIIVGHMGE MLPYMLERAS DMSTRWGGWG
PRDRPLRQVW DENIWITTSG SWSLAPLKCI LHNTKVERIM YSVDYPFESN ERGLEWFKEL
EGSGLLTEEQ LEMVAYRNAE DLLKVHMKKE Q
