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Methyltransferase tpcM (EC 2.1.1.-) (Geodin synthesis protein G)

 TPCM_ASPFU              Reviewed;         319 AA.
Q4WQY5;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
20-JUN-2018, entry version 59.
RecName: Full=Methyltransferase tpcM {ECO:0000303|PubMed:26242966};
EC=2.1.1.- {ECO:0000269|PubMed:26242966};
AltName: Full=Geodin synthesis protein G {ECO:0000303|PubMed:26242966};
Name=tpcM {ECO:0000303|PubMed:26242966};
Synonyms=tynM {ECO:0000303|PubMed:26278536}; ORFNames=AFUA_4G14460;
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.
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:0000305|PubMed:26278536}.
-!- TISSUE SPECIFICITY: Specifically expressed in conidia
(PubMed:22319557). {ECO:0000305|PubMed:22319557}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily.
{ECO:0000305}.
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EMBL; AAHF01000005; EAL89349.1; -; Genomic_DNA.
RefSeq; XP_751387.1; XM_746294.1.
ProteinModelPortal; Q4WQY5; -.
SMR; Q4WQY5; -.
EnsemblFungi; EAL89349; EAL89349; AFUA_4G14460.
GeneID; 3509494; -.
KEGG; afm:AFUA_4G14460; -.
EuPathDB; FungiDB:Afu4g14460; -.
HOGENOM; HOG000216816; -.
InParanoid; Q4WQY5; -.
OMA; QDVWERI; -.
OrthoDB; EOG092C33WK; -.
Proteomes; UP000002530; Chromosome 4.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IGC:AspGD.
InterPro; IPR013216; Methyltransf_11.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF08241; Methyltransf_11; 1.
SUPFAM; SSF53335; SSF53335; 1.
2: Evidence at transcript level;
Complete proteome; Methyltransferase; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 319 Methyltransferase tpcM.
/FTId=PRO_0000437071.
REGION 63 155 Methyltransferase domain. {ECO:0000255}.
SEQUENCE 319 AA; 35534 MW; 68BE9E493A3D5182 CRC64;
MAVPQSIPPP TAAPIESKDQ VFARSKAFWD NYLRGRPQVP PSFFQRIYRY HREHGGRFGT
VHDVGAGIGP YAGELRSQFP HVIVSDIVPK NVQLAEAHLG RDGFRYRAAP VEVADDLPPG
SVDLAFATNV MHFADQHAAM QAIATQLRPG GTFACAGFGP ARFDDPDIQD VWERISQQGG
RILLGMAEHP PDTINVMSRS SKEYNVAPLE PQWFRPGALR IRLNMAQGGI TGLLPPERQQ
EVTDPDFAGP RDVVVYETNE EWRFETDWEG FLQHFRSFPH AGADPAAFTG LLQELKDLLD
EGRCLRGCWP ATLILATRR


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