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 27-MAR-2024, entry version 131. 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; Deinococcota; 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 / RC 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 / RC 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 SABIO-RK; P14385; -. 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 CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.90.220.10; Adenine-n6-DNA-methyltransferase Taqi, Chain A, domain 2; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom. DR InterPro; IPR021188; N6_DNA_MeTrfase_TaqI. DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR025931; TaqI_C. DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1. DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1. DR Pfam; PF07669; Eco57I; 1. DR Pfam; PF12950; TaqI_C; 1. DR PIRSF; PIRSF037236; Ade-sp_methyltransferase_TaqI; 1. DR PRINTS; PR00507; N12N6MTFRASE. DR SUPFAM; SSF116734; DNA methylase specificity domain; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 //