ACLM_ASPOR
ID ACLM_ASPOR Reviewed; 433 AA.
AC Q2UPB3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=O-methyltransferase aclM {ECO:0000303|PubMed:25302411};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE AltName: Full=Aspitochlorine biosynthesis protein M {ECO:0000303|PubMed:25302411};
GN Name=aclM {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000039;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=25302411; DOI=10.1002/anie.201407624;
RA Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT involves a cryptic amino acid conversion.";
RL Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual
CC halogenated spiro compound with distinctive antifungal properties due
CC to selective inhibition of protein biosynthesis, and which is also
CC active against bacteria, viruses, and murine tumor cells
CC (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is
CC responsible the formation of the diketopiperazine (DKP) core from the
CC condensation of 2 phenylalanine residues (PubMed:25302411). One Phe
CC residue is tailored into chlorotyrosine by hydroxylation and
CC chlorination, whereas the second Phe undergoes an unprecedented C-C
CC bond cleavage to be converted into glycine (PubMed:25302411). After
CC formation of the DKP, sulfur is incorporated into the DKP by
CC conjugation with glutathione by aclG, followed by its stepwise
CC degradation to the thiol by aclI, aclJ and aclK, and the dithiol
CC oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB,
CC aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as
CC tailoring enzymes to produce the intermediate dechloroaspirochlorine
CC (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine
CC by the halogenase aclH is the last step in the aspirochlorine pathway
CC (PubMed:25302411). {ECO:0000269|PubMed:25302411}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AP007154; BAE56602.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UPB3; -.
DR SMR; Q2UPB3; -.
DR EnsemblFungi; BAE56602; BAE56602; AO090001000039.
DR HOGENOM; CLU_005533_12_2_1; -.
DR OMA; MMMTANG; -.
DR Proteomes; UP000006564; Chromosome 2.
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 Coiled coil; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..433
FT /note="O-methyltransferase aclM"
FT /id="PRO_0000441199"
FT COILED 5..37
FT /evidence="ECO:0000255"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 311..313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 433 AA; 48796 MW; 9263A2D3AFE717A8 CRC64;
MDAPLTDAER TALQTSLEAL NRQVEATRNI LRSNSQKALL QTLHTDQELP DPALEALAGK
TINLLHETQQ LLEPGHLVLA DHFLGYVSTK CLCAAVELKL VDILADADEA GMTVDELADA
SGAHPDRLQQ VLRVLRNDNI FDYDAVSHRY RNNRVSALLH SEHWTQWHNW VDLYGNEFYD
IARGIPRSIR REEARWAAQI NFDTNDDMFT YFQAQGWLPR LHRTLGGGAI AQAPGIVADY
PWHEIGSRTV LDVGGGGGGF LASLLREYPQ MRGGILDLPR TIEHACTLFH EPQGPYFDLR
ERVPRENLIA GDFLKAVPAF EIYTMKWVLH DWKDPDVLTI LRCIRASLIP GPDSRLVILE
SNLSDGQMGR LSRYGDINMM MTANGQERSE EQWRALAAAS GWEVSRIYPM RRAWVCAIDL
RPSASESGDR KHS
