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Database: UniProt
Entry: A0A1A1Y6Y5_9MYCO
LinkDB: A0A1A1Y6Y5_9MYCO
Original site: A0A1A1Y6Y5_9MYCO 
ID   A0A1A1Y6Y5_9MYCO        Unreviewed;       278 AA.
AC   A0A1A1Y6Y5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:OBF27081.1};
GN   ORFNames=A5724_03245 {ECO:0000313|EMBL:OBF27081.1};
OS   Mycobacterium sp. ACS1612.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF27081.1, ECO:0000313|Proteomes:UP000092025};
RN   [1] {ECO:0000313|Proteomes:UP000092025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA   Musoke P., Ssengooba W., Joloba M.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of the lipid moiety of the
CC       intermediate compounds phthiotriol and glycosylated phenolphthiotriol
CC       dimycoserosates to form phthiocerol dimycocerosates (DIM A) and
CC       glycosylated phenolphthiocerol dimycocerosates (PGL).
CC       {ECO:0000256|ARBA:ARBA00037600}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00038330}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBF27081.1}.
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DR   EMBL; LZHZ01000067; OBF27081.1; -; Genomic_DNA.
DR   RefSeq; WP_067810523.1; NZ_LZHZ01000067.1.
DR   AlphaFoldDB; A0A1A1Y6Y5; -.
DR   STRING; 1834117.A5724_03245; -.
DR   OrthoDB; 9769602at2; -.
DR   Proteomes; UP000092025; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR44068:SF11; GERANYL DIPHOSPHATE 2-C-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR44068; ZGC:194242; 1.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Methyltransferase {ECO:0000313|EMBL:OBF27081.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW   Transferase {ECO:0000313|EMBL:OBF27081.1}.
FT   DOMAIN          93..187
FT                   /note="Methyltransferase type 11"
FT                   /evidence="ECO:0000259|Pfam:PF08241"
SQ   SEQUENCE   278 AA;  32087 MW;  AD15AFDB42BD2428 CRC64;
     MSRSPLQTLD RIGVGLVYRI GSTATYKKVF KYWYPFMTRR LVGHEDVVFL NWGYEEDPPM
     GLPLDESDEP NRYSIQLYHQ TATQIDLSGK KVLEVSCGHG GGASYLMRTL HPDSYTALDF
     NSAAIEFCRK RHNLPGLDFV QGDAQSLPFP DESFDAVINV EASHIYPDFD RFVREVVRVL
     RPGGHFLHAD FRNRDNFPAW EAGLTQPPLR LISEKIINDQ VLRGLRKNSP RSNELINRYS
     PPFLRRFGRE FAVVDGSMFY KDLERGEIHY RTYCLTKD
//
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