Y4497_MYCVP
ID Y4497_MYCVP Reviewed; 226 AA.
AC A1TDM2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Putative O-methyltransferase Mvan_4497;
DE EC=2.1.1.-;
GN OrderedLocusNames=Mvan_4497;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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=ABM15272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000511; ABM15272.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041306948.1; NC_008726.1.
DR AlphaFoldDB; A1TDM2; -.
DR SMR; A1TDM2; -.
DR STRING; 350058.Mvan_4497; -.
DR EnsemblBacteria; ABM15272; ABM15272; Mvan_4497.
DR KEGG; mva:Mvan_4497; -.
DR eggNOG; COG4122; Bacteria.
DR HOGENOM; CLU_067676_2_0_11; -.
DR OrthoDB; 1948290at2; -.
DR Proteomes; UP000009159; Chromosome.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..226
FT /note="Putative O-methyltransferase Mvan_4497"
FT /id="PRO_0000380107"
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; 23157 MW; 9B571A31DF95A6BE CRC64;
MASTDEPGVG SGDPTARARQ AEAIVNHAEH SISEDAIVAA ARERAVDIGA GAVSPAVGAL
LCVLAKLTGA RAVVEVGTGA GVSGLWLLSG MREDGVLTTI DVEPEHQRIA KQAFSEAGVG
PGRTRLISGR AQEVLTRLAD ESYDLVFIDA APADQPHFVT EGVRLLRPGG AIVVHRAALG
GRAGDATAKD SEVAAVREAA RLIAEDDRLT PVLIPLGDGL LAAARD
