Y2199_MYCGI
ID Y2199_MYCGI Reviewed; 226 AA.
AC A4T8W9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Putative O-methyltransferase Mflv_2199;
DE EC=2.1.1.-;
GN OrderedLocusNames=Mflv_2199;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABP44677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000656; ABP44677.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041799973.1; NC_009338.1.
DR AlphaFoldDB; A4T8W9; -.
DR SMR; A4T8W9; -.
DR STRING; 350054.Mflv_2199; -.
DR EnsemblBacteria; ABP44677; ABP44677; Mflv_2199.
DR KEGG; mgi:Mflv_2199; -.
DR eggNOG; COG4122; Bacteria.
DR HOGENOM; CLU_067676_2_0_11; -.
DR OrthoDB; 1948290at2; -.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 3: Inferred from homology;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..226
FT /note="Putative O-methyltransferase Mflv_2199"
FT /id="PRO_0000380095"
FT BINDING 53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 77..78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 23138 MW; 6BD4F09377D0413E CRC64;
MASTDEPAAA SGDSTARARQ AEAIVNHAEH SISEDAIVAA ARERAVDIGA GAVTPAVGAL
LCVLAKLTGA KAVVEVGTGA GVSGLWLLSG MREDGVLTTI DVEPEHQRIA KQAFSEAGVG
PGRTRLISGR AQEVLTRLAD ESYDLVFIDA APADQPQFVV EGVRLLRPGG AIVVHRAALG
GRAGDASAKD SEVSAVREAA RLIAEDERLT PVLIPLGDGL LAAARD
