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Atrochrysone carboxyl ACP thioesterase (ACTE) (EC 3.1.-.-) (Monodictyphenone synthesis protein F)

 MDPF_EMENI              Reviewed;         307 AA.
Q5BH31; C8VQ67;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
05-DEC-2018, entry version 81.
RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000303|PubMed:20139316};
Short=ACTE {ECO:0000303|PubMed:20139316};
EC=3.1.-.- {ECO:0000269|PubMed:20139316};
AltName: Full=Monodictyphenone synthesis protein F {ECO:0000303|PubMed:20139316};
Name=mdpF {ECO:0000303|PubMed:20139316}; ORFNames=AN0149;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[2]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20139316; DOI=10.1128/AEM.02187-09;
Chiang Y.M., Szewczyk E., Davidson A.D., Entwistle R., Keller N.P.,
Wang C.C., Oakley B.R.;
"Characterization of the Aspergillus nidulans monodictyphenone gene
cluster.";
Appl. Environ. Microbiol. 76:2067-2074(2010).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21351751; DOI=10.1021/ja1096682;
Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S.,
Chiang Y.M., Wang C.C., Oakley B.R.;
"Genome-based deletion analysis reveals the prenyl xanthone
biosynthesis pathway in Aspergillus nidulans.";
J. Am. Chem. Soc. 133:4010-4017(2011).
-!- FUNCTION: Atrochrysone carboxyl ACP thioesterase; part of the gene
cluster that mediates the biosynthesis of monodictyphenone, a
prenyl xanthone derivative (PubMed:20139316, PubMed:21351751). The
pathway begins with the synthesis of atrochrysone thioester by the
polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone
carboxyl ACP thioesterase mdpF then breaks the thioester bond and
releases the atrochrysone carboxylic acid from mdpG
(PubMed:20139316). The atrochrysone carboxylic acid is then
converted to atrochrysone which is further transformed into emodin
anthrone (PubMed:20139316). The next step is performed by the
anthrone oxygenase mdpH that catalyzes the oxidation of
emodinanthrone to emodin (By similarity). Emodin is further
modified to yield monodictyphenone via several steps involving
mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
{ECO:0000250|UniProtKB:Q0CCY4, ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q988B9};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:Q988B9};
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:20139316}.
-!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone
and any of the intermediates of the pathway (PubMed:20139316,
PubMed:21351751). {ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
{ECO:0000305}.
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EMBL; BN001308; CBF90099.1; -; Genomic_DNA.
EMBL; AACD01000005; EAA66022.1; -; Genomic_DNA.
RefSeq; XP_657753.1; XM_652661.1.
ProteinModelPortal; Q5BH31; -.
SMR; Q5BH31; -.
STRING; 162425.CADANIAP00002594; -.
EnsemblFungi; CBF90099; CBF90099; ANIA_00149.
EnsemblFungi; EAA66022; EAA66022; AN0149.2.
GeneID; 2875922; -.
KEGG; ani:AN0149.2; -.
HOGENOM; HOG000246879; -.
InParanoid; Q5BH31; -.
OMA; PDLIRMY; -.
OrthoDB; EOG092C4LEI; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
Pfam; PF00753; Lactamase_B; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
3: Inferred from homology;
Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc.
CHAIN 1 307 Atrochrysone carboxyl ACP thioesterase.
/FTId=PRO_0000437055.
ACT_SITE 108 108 Proton donor/acceptor. {ECO:0000255}.
METAL 104 104 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 106 106 Zinc 1; via pros nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 108 108 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 109 109 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
SEQUENCE 307 AA; 33839 MW; 21F320C217C4CAB3 CRC64;
MAQPQQHKGG YKQINKALNI CAFEDYLSAQ LKHLPQLADV EQLSPRVIRV LGQNAGKGTN
TYIVGTGPQR LIIDTGQGIP EWADILDATL KERSISLSHV FLSHWHGDHT GGVPDLLRLY
PNLAGAIYKN SPGSDQQPID DGQVFRVEGA TIRAVHGPGH SHDHMCFILE EENAMFTGDN
VLGHGTSAVE ELGVYMETLR KLNSHHCAVG YPAHGDVITN LPAKIAGELA QKMRREKQVL
LTLDRINKES RRTGQVVLVH GDGIDEEVRK MALEPFIDEV LRKLAEDGKV AFEMRGGVKR
WFGVGVL


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