bifunctional alpha/beta hydrolase/class I SAM-dependent

LOCUS       WP_000431834             585 aa            linear   BCT 21-MAR-2023
            methyltransferase [Escherichia coli].
ACCESSION   WP_000431834
VERSION     WP_000431834.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Carr,P.D. and Ollis,D.L.
  TITLE     Alpha/beta hydrolase fold: an update
  JOURNAL   Protein Pept Lett 16 (10), 1137-1148 (2009)
   PUBMED   19508187
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Schubert,H.L., Blumenthal,R.M. and Cheng,X.
  TITLE     Many paths to methyltransfer: a chronicle of convergence
  JOURNAL   Trends Biochem Sci 28 (6), 329-335 (2003)
   PUBMED   12826405
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Martin,J.L. and McMillan,F.M.
  TITLE     SAM (dependent) I AM: the S-adenosylmethionine-dependent
            methyltransferase fold
  JOURNAL   Curr Opin Struct Biol 12 (6), 783-793 (2002)
   PUBMED   12504684
  REMARK    Erratum:[Curr Opin Struct Biol. 2003 Feb;13(1):142]
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Holmquist,M.
  TITLE     Alpha/Beta-hydrolase fold enzymes: structures, functions and
            mechanisms
  JOURNAL   Curr Protein Pept Sci 1 (2), 209-235 (2000)
   PUBMED   12369917
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 12114409
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..585
                     /product="bifunctional alpha/beta hydrolase/class I
                     SAM-dependent methyltransferase"
                     /EC_number="2.1.1.-"
                     /EC_number="3.-.-.-"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /GO_function="GO:1904047 - S-adenosyl-L-methionine binding
                     [Evidence IEA]"
                     /calculated_mol_wt=65269
     Region          32..265
                     /region_name="Hydrolase_4"
                     /note="Serine aminopeptidase, S33; pfam12146"
                     /db_xref="CDD:463473"
     Region          275..582
                     /region_name="Methyltransf_20"
                     /note="Putative methyltransferase; pfam12147"
                     /db_xref="CDD:432362"
     Site            order(414..420,439..440,466..468,487)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
ORIGIN      
        1 mensripgeh ffttsdntal fyrhwpalqp gakkvivlfh rghehsgrlq hivdelampd
       61 tafyawdarg hgqtsgprgy spslarsvrd vdefvrfaas dsqvgleevv viaqsvgavl
      121 vatwvhdyap airglvlasp afkvklyvpl arpalalwhr lrglffinsy vkgrylthdr
      181 qrvasfnndp litraiavni lldlyktser ivsdaaaitl ptqllisgdd yvvhrqpqid
      241 fyhrlrsplk elhllpgfyh dtlgeenraq afekmqsfis rlyanksqkf dyqhedrtgp
      301 sadrwrllsg gpvplspvdl ayrfmrkamk lfgthsaglh lgmstgfdsg ssldyvyqnq
      361 pqgsnafgrl idkiylnsvg wrgirqrkth lqilikqava dlhakglavr vvdiaaghgr
      421 yvldalanep avsdillrdy selnvaqgqe miaqrgmsgr vrfeqgdafn peelsaltpr
      481 ptlaivsgly elfpgneqvk nslaglanai epggillytg qpwhpqleli agvltshkdg
      541 kpwvmrvrsq gemdslvrda gfdkctqrid ewgiftvsma vrrdn