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Atrochrysone carboxyl ACP thioesterase (ACTE) (EC 3.1.-.-) (Trypacidin synthesis protein B)

 TPCB_ASPFU              Reviewed;         421 AA.
Q4WQZ6;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
20-JUN-2018, entry version 60.
RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000250|UniProtKB:Q0CCY4};
Short=ACTE {ECO:0000250|UniProtKB:Q0CCY4};
EC=3.1.-.- {ECO:0000250|UniProtKB:Q0CCY4};
AltName: Full=Trypacidin synthesis protein B {ECO:0000303|PubMed:26242966};
Name=tpcB {ECO:0000303|PubMed:26242966};
Synonyms=tynB {ECO:0000303|PubMed:26278536}; ORFNames=AFUA_4G14570;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
[2]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22319557; DOI=10.1371/journal.pone.0029906;
Gauthier T., Wang X., Sifuentes Dos Santos J., Fysikopoulos A.,
Tadrist S., Canlet C., Artigot M.P., Loiseau N., Oswald I.P., Puel O.;
"Trypacidin, a spore-borne toxin from Aspergillus fumigatus, is
cytotoxic to lung cells.";
PLoS ONE 7:E29906-E29906(2012).
[3]
FUNCTION.
PubMed=26278536; DOI=10.1007/s00253-015-6898-1;
Mattern D.J., Schoeler H., Weber J., Novohradska S., Kraibooj K.,
Dahse H.M., Hillmann F., Valiante V., Figge M.T., Brakhage A.A.;
"Identification of the antiphagocytic trypacidin gene cluster in the
human-pathogenic fungus Aspergillus fumigatus.";
Appl. Microbiol. Biotechnol. 99:10151-10161(2015).
[4]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=26242966; DOI=10.1111/1462-2920.13007;
Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
"Redundant synthesis of a conidial polyketide by two distinct
secondary metabolite clusters in Aspergillus fumigatus.";
Environ. Microbiol. 18:246-259(2016).
-!- FUNCTION: Atrochrysone carboxyl ACP thioesterase; part of the gene
cluster that mediates the biosynthesis of trypacidin, a mycotoxin
with antiprotozoal activity and that plays a role in the infection
process (PubMed:26278536, PubMed:26242966). The pathway begins
with the synthesis of atrochrysone thioester by the polyketide
synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl
ACP thioesterase tpcB then breaks the thioester bond and releases
the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The
decarboxylase tpcK converts atrochrysone carboxylic acid to
atrochrysone which is further reduced into emodin anthrone
(PubMed:26242966). The next step is performed by the emodin
anthrone oxygenase tpcL that catalyzes the oxidation of
emodinanthrone to emodin (PubMed:26242966). Emodin O-
methyltransferase encoded by tpcA catalyzes methylation of the 8-
hydroxy group of emodin to form questin (PubMed:26242966). Ring
cleavage of questin by questin oxidase tpcI leads to
desmethylsulochrin via several intermediates including questin
epoxide (By similarity). Another methylation step catalyzed by
tpcM leads to the formation of sulochrin which is further
converted to monomethylsulfochrin by tpcH. Finally, the tpcJ
catalyzes the conversion of monomethylsulfochrin to trypacidin
(PubMed:26242966). Trypacidin is toxic for human pulmonary and
bronchial epithelial cells by initiating the intracellular
formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)),
thus triggering host necrotic cell death (PubMed:22319557). The
trypacidin pathway is also able to produce endocrocin via a
distinct route from the endocrocin Enc pathway (PubMed:26242966).
{ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:22319557,
ECO:0000269|PubMed:26242966, ECO:0000269|PubMed:26278536}.
-!- 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:26242966, ECO:0000269|PubMed:26278536}.
-!- TISSUE SPECIFICITY: Specifically expressed in conidia
(PubMed:22319557). {ECO:0000305|PubMed:22319557}.
-!- INDUCTION: Expression is positively regulated by the transcription
factors brlA and laeA (PubMed:26242966).
{ECO:0000269|PubMed:26242966}.
-!- DISRUPTION PHENOTYPE: Impairs the production of trypacidin and
pathway intermediates including questin (PubMed:26278536,
PubMed:26242966). {ECO:0000269|PubMed:26242966,
ECO:0000269|PubMed:26278536}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
{ECO:0000305}.
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EMBL; AAHF01000005; EAL89338.1; -; Genomic_DNA.
RefSeq; XP_751376.1; XM_746283.1.
ProteinModelPortal; Q4WQZ6; -.
SMR; Q4WQZ6; -.
EnsemblFungi; EAL89338; EAL89338; AFUA_4G14570.
GeneID; 3509594; -.
KEGG; afm:AFUA_4G14570; -.
EuPathDB; FungiDB:Afu4g14570; -.
HOGENOM; HOG000246879; -.
InParanoid; Q4WQZ6; -.
OMA; RGGYRQI; -.
OrthoDB; EOG092C4LEI; -.
Proteomes; UP000002530; Chromosome 4.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
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.
2: Evidence at transcript level;
Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc.
CHAIN 1 421 Atrochrysone carboxyl ACP thioesterase.
/FTId=PRO_0000437056.
ACT_SITE 211 211 Proton donor/acceptor. {ECO:0000255}.
METAL 207 207 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 209 209 Zinc 1; via pros nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 211 211 Zinc 2; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
METAL 212 212 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250|UniProtKB:Q988B9}.
SEQUENCE 421 AA; 47062 MW; D7806C9437720360 CRC64;
MLALHQTQRD VPCSEVHDAL GLQGARSIYF GRPTGRSILS DPIRPRPMPT VTVIIYSDIR
FLLEFPSVFL CAYVLPVQRT VIMANEKRGG YRQINQALNI CAWEGYLNEQ HARLPTLEDV
EQISPRVLRV LGQNEGKVRR ADGYYTCSSR LIEGPQFTLQ GTNTYIVGTG RHRLLIDTGQ
GIPEWASLIS STLAGSSIEL SHVLLTHWHG DHTGGVPDLL RMYPDLSDSI YKHTPGKGQK
PISDGQTFRV EGATVRAVHT PGHSHDHMCF ILEEENAMFT GDNVLGHGSS AVEVLSTWMS
SLRMMQSLRC AVGYPAHGAV IRDLPSKLDL ELTQKARRED RVVETLKQMK TETQRNGARG
KGSVTVQQLV TAMHGHDLDE QVRTMALEPF VDEVLRKLAQ DDRVAFEVRG GQKKWFAIEY
T


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