CAMT_MYCTU
ID CAMT_MYCTU Reviewed; 220 AA.
AC O07431; F2GLY5; I6WXN4; L0T2S4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Catechol O-methyltransferase {ECO:0000303|PubMed:31147608};
DE Short=COMT {ECO:0000303|PubMed:31147608};
DE EC=2.1.1.6 {ECO:0000269|PubMed:31147608};
GN OrderedLocusNames=Rv0187 {ECO:0000312|EMBL:CCP42914.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND STRONTIUM ION, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF LYS-142.
RC STRAIN=H37Rv;
RX PubMed=31147608; DOI=10.1038/s41598-019-44592-7;
RA Lee S., Kang J., Kim J.;
RT "Structural and biochemical characterization of Rv0187, an O-
RT methyltransferase from Mycobacterium tuberculosis.";
RL Sci. Rep. 9:8059-8059(2019).
CC -!- FUNCTION: Catechol O-methyltransferase that can use various catechol-
CC like compounds such as gallic acid (GA), 3,4-dihydroxy-5-methoxy-
CC benzoic acid (5OMeBA), protocatechuic acid (PCA), 3,4-dihydroxy-
CC benzaldehyde (DHA), dopamine, caffeic acid (CA), luteolin, quercetin,
CC and 5-hydroxyuridine. {ECO:0000269|PubMed:31147608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134251; EC=2.1.1.6;
CC Evidence={ECO:0000269|PubMed:31147608};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:31147608};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:31147608}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.030 mM for 5OMeBA {ECO:0000269|PubMed:31147608};
CC KM=0.15 mM for PCA {ECO:0000269|PubMed:31147608};
CC KM=0.49 mM for CA {ECO:0000269|PubMed:31147608};
CC Note=kcat is 0.080 min(-1) with 5OMeBA as substrate. kcat is 0.22
CC min(-1) with PCA as substrate. kcat is 0.43 min(-1) with CA as
CC substrate. {ECO:0000269|PubMed:31147608};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31147608}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; AL123456; CCP42914.1; -; Genomic_DNA.
DR RefSeq; NP_214701.1; NC_000962.3.
DR RefSeq; WP_003401129.1; NZ_NVQJ01000001.1.
DR PDB; 6JCL; X-ray; 1.64 A; A/B/C/D/E/F/G/H=1-220.
DR PDB; 6JCM; X-ray; 2.08 A; A/B/C/D=3-220.
DR PDBsum; 6JCL; -.
DR PDBsum; 6JCM; -.
DR AlphaFoldDB; O07431; -.
DR SMR; O07431; -.
DR STRING; 83332.Rv0187; -.
DR PaxDb; O07431; -.
DR PRIDE; O07431; -.
DR DNASU; 886779; -.
DR GeneID; 886779; -.
DR KEGG; mtu:Rv0187; -.
DR PATRIC; fig|83332.111.peg.215; -.
DR TubercuList; Rv0187; -.
DR eggNOG; COG4122; Bacteria.
DR OMA; MGEHPRL; -.
DR PhylomeDB; O07431; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016206; F:catechol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102084; F:L-dopa O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102938; F:orcinol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..220
FT /note="Catechol O-methyltransferase"
FT /id="PRO_0000448281"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000305|PubMed:31147608"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 68..69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000305|PubMed:31147608"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000305|PubMed:31147608"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000305|PubMed:31147608"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000305|PubMed:31147608"
FT BINDING 139
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|PubMed:31147608"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000305|PubMed:31147608"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|PubMed:31147608"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|PubMed:31147608"
FT MUTAGEN 142
FT /note="K->A: Retains a low but substantial activity."
FT /evidence="ECO:0000269|PubMed:31147608"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:6JCM"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:6JCL"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:6JCL"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:6JCL"
SQ SEQUENCE 220 AA; 23097 MW; 2FEBCCB37B0F9687 CRC64;
MGMDQQPNPP DVDAFLDSTL VGDDPALAAA LAASDAAELP RIAVSAQQGK FLCLLAGAIQ
ARRVLEIGTL GGFSTIWLAR GAGPQGRVVT LEYQPKHAEV ARVNLQRAGV ADRVEVVVGP
ALDTLPTLAG GPFDLVFIDA DKENNVAYIQ WAIRLARRGA VIVVDNVIRG GGILAESDDA
DAVAARRTLQ MMGEHPGLDA TAIQTVGRKG WDGFALALVR
