AMP-binding protein [Klebsiella pneumoniae].

LOCUS       WP_014342997             431 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_014342997
VERSION     WP_014342997.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Conti,E., Franks,N.P. and Brick,P.
  TITLE     Crystal structure of firefly luciferase throws light on a
            superfamily of adenylate-forming enzymes
  JOURNAL   Structure 4 (3), 287-298 (1996)
   PUBMED   8805533
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 :: NF012711.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00501.34
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..431
                     /product="AMP-binding protein"
                     /calculated_mol_wt=46779
     Region          5..420
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(71,74..79,81..82)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(74,191..192,213..218,306,318,321,332,412)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(74,116..117,164,166..167,170,191..192,213..218,306,
                     318,321,329..332,393)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(116,166..167,170,191,329..331,387,393)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
ORIGIN      
        1 mkccffdqtf lplvaqllpq lptvkhvvlm esrseaalsq lpsllfyddl lqqgmadyrw
       61 pqlneltpas lcytsgttgr pkgvlnthrs lvlhalsgnq pdaagisakd sllpvvpmfh
      121 vnawgtpfia amvgarlvlp gphldgdsll qllaaekvtv gfgvpviwag llaamrrtev
      181 rlpefkralv ggsalppsma eafqrdygia lthawgmtet spigtintpl skhdalpaqe
      241 qqkqcagqgr pifgielqvv dvdgeplprd gqsqgylqvr ghwvveqyyg qdasaltaag
      301 wfdtgdigtl dangylvisd rakdiiksgg ewistvelen iaiahpgvrs aaaiaarhpr
      361 wderpvllcv raeggeveet dllswfekrv pkwqipdrvi fvdalpvsat gkvlknqlrq
      421 aygeilmseg k