MULTISPECIES: bifunctional alpha/beta hydrolase/class I

LOCUS       WP_000431885             585 aa            linear   BCT 21-MAR-2023
            SAM-dependent methyltransferase [Shigella].
ACCESSION   WP_000431885
VERSION     WP_000431885.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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="Shigella"
                     /db_xref="taxon:620"
     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=65378
     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 yyrhwptlqp gakkvivlfh rghehsgrlq hlvdelampd
       61 tafyawdarg hgknsgprgy spslmrsvqd vdefvrfaas dsqvgleevv viaqsvgavl
      121 vatwvhdyap airglvlasp afkvklyvpl arpalalwhr lrglffinsy vkgrylthdr
      181 qrvasfnndp litraiavni lldlyktser ivsdaaaitl ptqllisgdd yvvhrqpqid
      241 fyqrlrsplk elhllpgfyh dtlgeenraq afekmqsfic rlyanksqkf dyqhedrtgp
      301 sadrwrllsg gpvplspvdl ayrfmrkamk lfgahsaglh lgmstgfdsg ssldyvyqnq
      361 pqgsnafgrl idkiylnsvg wrgirqrkth lqilikqava dlhakglavr vvdiaaghgr
      421 yvldalanep avsdillrdy selnvaqgqe miaqrgmsgr vrfeqgdafn peelsaltpr
      481 ptlaivsgly elfpeneqvk nslaglanai epggiliytg qpwhpqleli agvltshkdg
      541 kpwvmrvrsq gemdslvrna gfdkctqrid vwgiftvsma vrrdn