MTTA_THEAQ
ID MTTA_THEAQ Reviewed; 421 AA.
AC P14385;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Type II methyltransferase M.TaqI {ECO:0000303|PubMed:12654995};
DE Short=M.TaqI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.72 {ECO:0000269|PubMed:9931007};
DE AltName: Full=Adenine-specific methyltransferase TaqI;
DE AltName: Full=Modification methylase TaqI;
GN Name=taqIM;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=2827113; DOI=10.1093/nar/15.23.9781;
RA Slatko B.E., Benner J.S., Moran L.S., Jager-Quinton T., Simcox T.G.,
RA van Cott E.M., Wilson G.G.;
RT "Cloning, sequencing and expression of the Taq I restriction-modification
RT system.";
RL Nucleic Acids Res. 15:9781-9796(1987).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=1551602; DOI=10.1016/0378-1119(92)90307-b;
RA Barany F., Slatko B., Danzitz M., Cowburn D., Schildkraut I., Wilson G.G.;
RT "The corrected nucleotide sequences of the TaqI restriction and
RT modification enzymes reveal a thirteen-codon overlap.";
RL Gene 112:91-95(1992).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-108 AND PHE-196.
RX PubMed=9931007; DOI=10.1021/bi9818016;
RA Pues H., Bleimling N., Holz B., Wolcke J., Weinhold E.;
RT "Functional roles of the conserved aromatic amino acid residues at position
RT 108 (motif IV) and position 196 (motif VIII) in base flipping and catalysis
RT by the N6-adenine DNA methyltransferase from Thermus aquaticus.";
RL Biochemistry 38:1426-1434(1999).
RN [4]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH S-ADENOSYLMETHIONINE.
RX PubMed=7971991; DOI=10.1073/pnas.91.23.10957;
RA Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E.,
RA Schildkraut I., Saenger W.;
RT "Three-dimensional structure of the adenine-specific DNA methyltransferase
RT M.Taq I in complex with the cofactor S-adenosylmethionine.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:10957-10961(1994).
RN [6] {ECO:0007744|PDB:1AQI, ECO:0007744|PDB:1AQJ, ECO:0007744|PDB:2ADM}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYLHOMOCYSTEINE AND SINEFUNGIN, AND A REINTERPRETATION IN COMPLEX
RP WITH S-ADENOSYLMETHIONINE.
RX PubMed=8995524; DOI=10.1006/jmbi.1996.0711;
RA Schluckebier G., Kozak M., Bleimling N., Weinhold E., Saenger W.;
RT "Differential binding of S-adenosylmethionine S-adenosylhomocysteine and
RT sinefungin to the adenine-specific DNA methyltransferase M.TaqI.";
RL J. Mol. Biol. 265:56-67(1997).
RN [7] {ECO:0007744|PDB:1G38}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-413 IN COMPLEX WITH DNA, AND
RP DISCUSSION OF ENZYME MECHANISM.
RX PubMed=11175899; DOI=10.1038/84104;
RA Goedecke K., Pignot M., Goody R.S., Scheidig A.J., Weinhold E.;
RT "Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with
RT DNA and a cofactor analog.";
RL Nat. Struct. Biol. 8:121-125(2001).
CC -!- FUNCTION: A gamma subtype methylase that recognizes the double-stranded
CC sequence 5'-TCGA-3', methylates A-4 on both strands and protects the
CC DNA from cleavage by the TaqI endonuclease.
CC {ECO:0000269|PubMed:2827113, ECO:0000269|PubMed:9931007,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000269|PubMed:9931007};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for DNA {ECO:0000269|PubMed:9931007};
CC KM=3.7 uM for S-adenosylmethionine {ECO:0000269|PubMed:9931007};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00499; CAA68551.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M76681; AAA27506.1; -; Genomic_DNA.
DR PIR; JN0257; JN0257.
DR PDB; 1AQI; X-ray; 2.60 A; A/B=1-421.
DR PDB; 1AQJ; X-ray; 2.60 A; A/B=1-421.
DR PDB; 1G38; X-ray; 2.00 A; A/D=21-413.
DR PDB; 2ADM; X-ray; 2.60 A; A/B=1-421.
DR PDB; 2IBS; X-ray; 2.40 A; A/D=1-421.
DR PDB; 2IBT; X-ray; 1.70 A; A/D=1-421.
DR PDB; 2IH2; X-ray; 1.61 A; A/D=1-421.
DR PDB; 2IH4; X-ray; 2.10 A; A/D=1-421.
DR PDB; 2IH5; X-ray; 1.80 A; A=1-421.
DR PDB; 2JG3; X-ray; 1.90 A; A/D=1-421.
DR PDB; 2NP6; X-ray; 2.10 A; A/D=1-421.
DR PDB; 2NP7; X-ray; 1.90 A; A=1-421.
DR PDBsum; 1AQI; -.
DR PDBsum; 1AQJ; -.
DR PDBsum; 1G38; -.
DR PDBsum; 2ADM; -.
DR PDBsum; 2IBS; -.
DR PDBsum; 2IBT; -.
DR PDBsum; 2IH2; -.
DR PDBsum; 2IH4; -.
DR PDBsum; 2IH5; -.
DR PDBsum; 2JG3; -.
DR PDBsum; 2NP6; -.
DR PDBsum; 2NP7; -.
DR AlphaFoldDB; P14385; -.
DR SMR; P14385; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR DrugBank; DB01910; Sinefungin.
DR BRENDA; 2.1.1.72; 6334.
DR EvolutionaryTrace; P14385; -.
DR PRO; PR:P14385; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.90.220.10; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR021188; N6_DNA_MeTrfase_TaqI.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
DR InterPro; IPR011639; RM_methylase_Eco57I-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PIRSF; PIRSF037236; Ade-sp_methyltransferase_TaqI; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..421
FT /note="Type II methyltransferase M.TaqI"
FT /id="PRO_0000087980"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:2ADM"
FT BINDING 45..48
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:2ADM"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:2ADM"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:2ADM"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:2ADM"
FT SITE 105
FT /note="Important for catalytic activity"
FT /evidence="ECO:0007744|PDB:2ADM"
FT SITE 106
FT /note="Important for catalytic activity; via amide
FT nitrogen"
FT /evidence="ECO:0007744|PDB:2ADM"
FT SITE 108
FT /note="Important for catalytic activity"
FT /evidence="ECO:0007744|PDB:2ADM"
FT MUTAGEN 108
FT /note="Y->A,G: Drastically reduces enzymatic activity; KM
FT for both DNA and s-adenosylmethionine is not significantly
FT changed."
FT /evidence="ECO:0000269|PubMed:9931007"
FT MUTAGEN 108
FT /note="Y->F,W: Essentially wild-type activity."
FT /evidence="ECO:0000269|PubMed:9931007"
FT MUTAGEN 196
FT /note="F->A: Drastically reduces enzymatic activity; KM for
FT both DNA and s-adenosylmethionine is not significantly
FT changed."
FT /evidence="ECO:0000269|PubMed:9931007"
FT MUTAGEN 196
FT /note="F->W: Essentially wild-type activity."
FT /evidence="ECO:0000269|PubMed:9931007"
FT CONFLICT 13
FT /note="S -> A (in Ref. 1; CAA68551)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> G (in Ref. 1; AAA27506)"
FT /evidence="ECO:0000305"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:2IH2"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2IH2"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1AQI"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 316..321
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2IH2"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1AQI"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:2IH2"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:2IH2"
SQ SEQUENCE 421 AA; 47862 MW; 21C62B53C43DB7FF CRC64;
MGLPPLLSLP SNSAPRSLGR VETPPEVVDF MVSLAEAPRG GRVLEPACAH GPFLRAFREA
HGTAYRFVGV EIDPKALDLP PWAEGILADF LLWEPGEAFD LILGNPPYGI VGEASKYPIH
VFKAVKDLYK KAFSTWKGKY NLYGAFLEKA VRLLKPGGVL VFVVPATWLV LEDFALLREF
LAREGKTSVY YLGEVFPQKK VSAVVIRFQK SGKGLSLWDT QESESGFTPI LWAEYPHWEG
EIIRFETEET RKLEISGMPL GDLFHIRFAA RSPEFKKHPA VRKEPGPGLV PVLTGRNLKP
GWVDYEKNHS GLWMPKERAK ELRDFYATPH LVVAHTKGTR VVAAWDERAY PWREEFHLLP
KEGVRLDPSS LVQWLNSEAM QKHVRTLYRD FVPHLTLRML ERLPVRREYG FHTSPESARN
F
