XANE_ASPFU
ID XANE_ASPFU Reviewed; 431 AA.
AC Q4WED7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=O-methyltransferase xanE {ECO:0000303|PubMed:29844112};
DE EC=2.1.1.- {ECO:0000305|PubMed:29844112};
DE AltName: Full=Xanthocillin biosynthesis cluster protein E {ECO:0000303|PubMed:29844112};
GN Name=xanE {ECO:0000303|PubMed:29844112}; ORFNames=AFUA_5G02640;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=29844112; DOI=10.1128/mbio.00785-18;
RA Lim F.Y., Won T.H., Raffa N., Baccile J.A., Wisecaver J., Rokas A.,
RA Schroeder F.C., Keller N.P.;
RT "Fungal isocyanide synthases and xanthocillin biosynthesis in Aspergillus
RT fumigatus.";
RL MBio 9:0-0(2018).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of the isocyanide xanthocillin and its derivatives
CC (PubMed:29844112). The first step of the pathway consists in the
CC conversion of tyrosine into a vinyl-isonitrile intermediate by the
CC isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative
CC dimerization of this intermediate to form xanthocillin may involve the
CC cytochrome P450 monooxygenase xanG, whose expression is coregulated
CC with that of XanB (PubMed:29844112). Xanthocillin can be further
CC modified by the isonitrile hydratase-like protein xanA which introduces
CC N-formyl groups and the methyltransferase xanE which introduces methyl
CC groups, leading to the production of several derivatives including
CC fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject
CC to both oxidative and reductive cyclization to yield melanocins E and
CC F, respectively (PubMed:29844112). {ECO:0000269|PubMed:29844112}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:29844112}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL86040.1; -; Genomic_DNA.
DR RefSeq; XP_748078.1; XM_742985.1.
DR AlphaFoldDB; Q4WED7; -.
DR SMR; Q4WED7; -.
DR EnsemblFungi; EAL86040; EAL86040; AFUA_5G02640.
DR GeneID; 3505486; -.
DR KEGG; afm:AFUA_5G02640; -.
DR VEuPathDB; FungiDB:Afu5g02640; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_1_2_1; -.
DR InParanoid; Q4WED7; -.
DR OMA; LISHACD; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..431
FT /note="O-methyltransferase xanE"
FT /id="PRO_0000445297"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 431 AA; 47750 MW; 1A8602775A218751 CRC64;
MSTQHGPKST RTNDLYELAV NISSTVEAFV GRLDAIGAER PNLDNPFPEI IQDEGAQLAR
LKILRLCERL MALVQGPVQW LMFQNMAFLD AACVGAILDM GIHDIIAPGP EPTSLDQIVE
ATGASKDILK RIMRVCTQRL VFDEIAPEQF IHNGVSLQFL APPVQALISH ACDDGLRMAA
HFTDSLKKTD WKGSDDPENT AFSLAFNTNK GLFDYFYTED LARGQRFALG MAGSEIMKTL
TEDMFPFESL PQGAKVVDVG GGRGHVSVRI AEKVPGLNFV VQDDESMLEA GQAEGVPKAV
KDRIEFMPHD FFNEQPVKGA DVYLLRFILH DHSDSRCAKI LSNIVDAMEP GKSRILIDDA
IVPSFLGPES SRFFNLLDLY MLAGLNGKER TLEQWNYLIQ MVSPKLVLEK VWKTPNGGPE
SGTILELRLQ E
