MET1_MYCHD
ID MET1_MYCHD Reviewed; 218 AA.
AC K5B7F3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=MMP 1-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.365 {ECO:0000269|PubMed:30606802};
DE AltName: Full=3-O-methylmannose polysaccharide 1-O-methyltransferase {ECO:0000305};
GN Name=meT1 {ECO:0000303|PubMed:30606802};
GN ORFNames=C731_4163 {ECO:0000312|EMBL:EKF21848.1},
GN MHAS_04405 {ECO:0000312|EMBL:VCT92675.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
RX PubMed=23209251; DOI=10.1128/jb.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
RX PubMed=30701245; DOI=10.1128/mra.01522-18;
RA Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL Microbiol. Resour. Announc. 8:e01522-e01522(2019).
RN [3] {ECO:0007744|PDB:6G7D, ECO:0007744|PDB:6G80, ECO:0007744|PDB:6H40}
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND MAGNESIUM ION, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP ACTIVE SITE, AND MUTAGENESIS OF GLU-78; HIS-79 AND HIS-144.
RX PubMed=30606802; DOI=10.1073/pnas.1813450116;
RA Ripoll-Rozada J., Costa M., Manso J.A., Maranha A., Miranda V.,
RA Sequeira A., Ventura M.R., Macedo-Ribeiro S., Pereira P.J.B.,
RA Empadinhas N.;
RT "Biosynthesis of mycobacterial methylmannose polysaccharides requires a
RT unique 1-O-methyltransferase specific for 3-O-methylated mannosides.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:835-844(2019).
CC -!- FUNCTION: Involved in the biosynthesis of 3-O-methylmannose
CC polysaccharides (MMP), which are intracellular polymethylated
CC polysaccharides implicated in the modulation of fatty acid metabolism
CC in non-tuberculous mycobacteria (PubMed:30606802). Specifically
CC methylates the 1-OH position of 3,3'-di-O-methyl-4alpha-mannobiose, a
CC probable early precursor of MMP, yielding the reducing end dimannoside
CC of MMP (PubMed:30606802). {ECO:0000269|PubMed:30606802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,3'-di-O-methyl-4alpha-mannobiose + S-adenosyl-L-methionine =
CC 1,3,3'-tri-O-methyl-4alpha-mannobiose + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:62408, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:145745,
CC ChEBI:CHEBI:145746; EC=2.1.1.365;
CC Evidence={ECO:0000269|PubMed:30606802};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62409;
CC Evidence={ECO:0000269|PubMed:30606802};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30606802};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:30606802}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for 3,3'-di-O-methyl-4alpha-mannobiose
CC {ECO:0000269|PubMed:30606802};
CC KM=0.055 mM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:30606802};
CC Vmax=75 nmol/min/mg enzyme toward 3,3'-di-O-methyl-4alpha-mannobiose
CC {ECO:0000269|PubMed:30606802};
CC Vmax=85 nmol/min/mg enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:30606802};
CC Note=kcat is 0.037 min(-1). {ECO:0000269|PubMed:30606802};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:30606802};
CC Temperature dependence:
CC Optimum temperature is 50-55 degrees Celsius.
CC {ECO:0000269|PubMed:30606802};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30606802}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AMRA01000112; EKF21848.1; -; Genomic_DNA.
DR EMBL; LR026975; VCT92675.1; -; Genomic_DNA.
DR RefSeq; WP_005631133.1; NZ_LR026975.1.
DR PDB; 6G7D; X-ray; 1.35 A; A=1-218.
DR PDB; 6G80; X-ray; 2.05 A; A/B/C/M=1-218.
DR PDB; 6H40; X-ray; 1.05 A; A=1-218.
DR PDBsum; 6G7D; -.
DR PDBsum; 6G80; -.
DR PDBsum; 6H40; -.
DR AlphaFoldDB; K5B7F3; -.
DR SASBDB; K5B7F3; -.
DR SMR; K5B7F3; -.
DR STRING; 1122247.C731_4163; -.
DR EnsemblBacteria; EKF21848; EKF21848; C731_4163.
DR EnsemblBacteria; VCT92675; VCT92675; MHAS_04405.
DR KEGG; mhas:MHAS_04405; -.
DR PATRIC; fig|1122247.3.peg.3993; -.
DR eggNOG; COG4122; Bacteria.
DR OMA; YEGWAPH; -.
DR OrthoDB; 1948290at2; -.
DR BioCyc; MetaCyc:MON-21025; -.
DR BRENDA; 2.1.1.365; 15810.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR Proteomes; UP000268660; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Magnesium; Metal-binding;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..218
FT /note="MMP 1-O-methyltransferase"
FT /id="PRO_0000452108"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30606802"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:30606802"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30606802"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30606802"
FT MUTAGEN 78
FT /note="E->A: 87% decrease in activity. Decreases affinity
FT for both 3,3-dimethylmannobiose and S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:30606802"
FT MUTAGEN 79
FT /note="H->A: 85% decrease in activity. Decreases affinity
FT for both 3,3-dimethylmannobiose and S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:30606802"
FT MUTAGEN 144
FT /note="H->A: Loss of activity. Slightly affects the
FT affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:30606802"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:6G80"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6H40"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6H40"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:6H40"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6H40"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:6H40"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6H40"
SQ SEQUENCE 218 AA; 23890 MW; 4BB21BA43C5FD476 CRC64;
MTDIRDTDAL FALADRVTGF MPADEGRTLY ETAVRYLGDG VGVEIGTYCG KSTVLLGAAA
RQTGGVVFTV DHHHGSEEHQ PGWEYHDPSL VDPVTGLFDT LPRLRHTLDE ADLYDHVVAV
VGKSAVVARG WRTPLRFLFI DGGHTEEAAQ RDFDGWARWV EVGGALVIHD VFPDPKDGGQ
APFHIYQRAL NTGDFREVNA YGSMRVLERT SGIAGQPL
