MULTISPECIES: peptide deformylase [Klebsiella].

LOCUS       WP_002919144             169 aa            linear   BCT 06-JUN-2022
ACCESSION   WP_002919144
VERSION     WP_002919144.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Meinnel,T., Lazennec,C., Villoing,S. and Blanquet,S.
  TITLE     Structure-function relationships within the peptide deformylase
            family. Evidence for a conserved architecture of the active site
            involving three conserved motifs and a metal ion
  JOURNAL   J Mol Biol 267 (3), 749-761 (1997)
   PUBMED   9126850
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  :: HMM
            Evidence Accession :: TIGR00079.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..169
                     /gene="def"
     Protein         1..169
                     /product="peptide deformylase"
                     /EC_number="3.5.1.88"
                     /GO_function="GO:0042586 - peptide deformylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0036211 - protein modification process
                     [Evidence IEA]"
                     /calculated_mol_wt=19239
     Region          1..163
                     /region_name="def"
                     /note="peptide deformylase; Reviewed; PRK00150"
                     /db_xref="CDD:234668"
     Site            order(44..46,51,90..92,133..134,137)
                     /site_type="active"
                     /db_xref="CDD:238271"
     Site            order(46,51,92,134)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238271"
     Site            order(91,133,137)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238271"
ORIGIN      
        1 mavlqvlhip derlrkvaep vkevnaeiqr ivddmfdtmy aeegiglaat qvdihqriiv
       61 idvsenreeq lvlinpemle kdgetgieeg clsipeqral vpraekvkir alerdgkpfe
      121 leadgllaic iqhemdhlvg klfidylspl kqqrirqkve kldrlrsra