Y2640_MYCLE
ID Y2640_MYCLE Reviewed; 310 AA.
AC Q9CCZ4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase ML2640;
DE EC=2.1.1.-;
GN OrderedLocusNames=ML2640;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND FUNCTION.
RX PubMed=17660248; DOI=10.1110/ps.072982707;
RA Grana M., Haouz A., Buschiazzo A., Miras I., Wehenkel A., Bondet V.,
RA Shepard W., Schaeffer F., Cole S.T., Alzari P.M.;
RT "The crystal structure of M. leprae ML2640c defines a large family of
RT putative S-adenosylmethionine-dependent methyltransferases in
RT mycobacteria.";
RL Protein Sci. 16:1896-1904(2007).
CC -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC activity. {ECO:0000305|PubMed:17660248}.
CC -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR EMBL; AL583926; CAC32172.1; -; Genomic_DNA.
DR PIR; F87239; F87239.
DR RefSeq; NP_302690.1; NC_002677.1.
DR RefSeq; WP_010909009.1; NC_002677.1.
DR PDB; 2CKD; X-ray; 2.80 A; A/B=1-310.
DR PDB; 2UYO; X-ray; 1.70 A; A=1-310.
DR PDB; 2UYQ; X-ray; 1.80 A; A=1-310.
DR PDBsum; 2CKD; -.
DR PDBsum; 2UYO; -.
DR PDBsum; 2UYQ; -.
DR AlphaFoldDB; Q9CCZ4; -.
DR SMR; Q9CCZ4; -.
DR STRING; 272631.ML2640; -.
DR EnsemblBacteria; CAC32172; CAC32172; CAC32172.
DR KEGG; mle:ML2640; -.
DR PATRIC; fig|272631.5.peg.5067; -.
DR Leproma; ML2640; -.
DR eggNOG; COG3315; Bacteria.
DR HOGENOM; CLU_056160_2_1_11; -.
DR OMA; PMDITEL; -.
DR EvolutionaryTrace; Q9CCZ4; -.
DR PRO; PR:Q9CCZ4; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR011610; CHP00027_methylltransferase.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF04072; LCM; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..310
FT /note="Putative S-adenosyl-L-methionine-dependent
FT methyltransferase ML2640"
FT /id="PRO_0000356894"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:17660248"
FT BINDING 161..162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2CKD"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:2CKD"
FT HELIX 71..100
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:2UYO"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2CKD"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:2UYO"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:2UYO"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:2UYO"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2UYO"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:2UYO"
SQ SEQUENCE 310 AA; 34454 MW; 076DCA5DBB1DF78D CRC64;
MRTHDDTWDI KTSVGTTAVM VAAARAAETD RPDALIRDPY AKLLVTNTGA GALWEAMLDP
SMVAKVEAID AEAAAMVEHM RSYQAVRTNF FDTYFNNAVI DGIRQFVILA SGLDSRAYRL
DWPTGTTVYE IDQPKVLAYK STTLAEHGVT PTADRREVPI DLRQDWPPAL RSAGFDPSAR
TAWLAEGLLM YLPATAQDGL FTEIGGLSAV GSRIAVETSP LHGDEWREQM QLRFRRVSDA
LGFEQAVDVQ ELIYHDENRA VVADWLNRHG WRATAQSAPD EMRRVGRWGD GVPMADDKDA
FAEFVTAHRL
