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Anthrone oxygenase tpcL (EC 1.-.-.-) (Trypacidin synthesis protein L)

 TPCL_ASPFU              Reviewed;         161 AA.
Q4WQY6;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
20-JUN-2018, entry version 51.
RecName: Full=Anthrone oxygenase tpcL {ECO:0000303|PubMed:26242966};
EC=1.-.-.- {ECO:0000305|PubMed:26242966};
AltName: Full=Trypacidin synthesis protein L {ECO:0000303|PubMed:26242966};
Name=tpcL {ECO:0000303|PubMed:26242966};
Synonyms=tynL {ECO:0000303|PubMed:26278536}; ORFNames=AFUA_4G14480;
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, 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: Methyltransferase; 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:Q0CCX8, ECO:0000269|PubMed:22319557,
ECO:0000269|PubMed:26242966, ECO:0000269|PubMed:26278536}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:26242966}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
protein {ECO:0000255}.
-!- 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}.
-!- SIMILARITY: Belongs to the anthrone oxygenase family.
{ECO:0000305}.
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EMBL; AAHF01000005; EAL89348.2; -; Genomic_DNA.
RefSeq; XP_751386.2; XM_746293.2.
EnsemblFungi; EAL89348; EAL89348; AFUA_4G14480.
GeneID; 3509610; -.
KEGG; afm:AFUA_4G14480; -.
EuPathDB; FungiDB:Afu4g14480; -.
HOGENOM; HOG000216818; -.
InParanoid; Q4WQY6; -.
OMA; FRMHANP; -.
OrthoDB; EOG092C57S3; -.
Proteomes; UP000002530; Chromosome 4.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IGC:AspGD.
2: Evidence at transcript level;
Complete proteome; Glycoprotein; Membrane; Monooxygenase;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 161 Anthrone oxygenase tpcL.
/FTId=PRO_0000437098.
TRANSMEM 15 35 Helical. {ECO:0000255}.
TRANSMEM 56 74 Helical. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
TRANSMEM 136 155 Helical. {ECO:0000255}.
CARBOHYD 4 4 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
SEQUENCE 161 AA; 17361 MW; 4EF73E3BB7043B9E CRC64;
MPQNASVIIT QATAVITGSF LSGLMMGLSV VDIPVVLDTA TQASQLLQHF TRLYDIGHKM
MPSLAVTTCL LYGYTASSTR TTGGSGLPHI IAAVTTISMV PFTWLVMAPT NNALFRMHAN
PAAANLGEVR RLLVRWAQLH AVRSLFPLMG SVLGLRQILR E


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