MULTISPECIES: acyltransferase [Klebsiella].

LOCUS       WP_002884634             151 aa            linear   BCT 20-MAR-2023
ACCESSION   WP_002884634
VERSION     WP_002884634.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
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 10129729
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..151
                     /product="acyltransferase"
                     /EC_number="2.3.1.-"
                     /GO_function="GO:0016746 - acyltransferase activity
                     [Evidence IEA]"
                     /GO_function="GO:0120225 - coenzyme A binding [Evidence
                     IEA]"
                     /calculated_mol_wt=16210
     Region          31..149
                     /region_name="LbH_WxcM_N_like"
                     /note="WcxM-like, Left-handed parallel beta-Helix (LbH)
                     N-terminal domain: This group is composed of Xanthomonas
                     campestris WcxM and proteins with similarity to the WcxM
                     N-terminal domain. WcxM is thought to be bifunctional,
                     catalyzing both the isomerization...; cd03358"
                     /db_xref="CDD:100048"
     Site            order(52,54,62,70,72,78,84..85,87,104,106,109,127,143)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100048"
     Site            order(54,56,84,87,106,108..109,114,125..126,131..132,
                     141..142,144)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:100048"
     Site            order(54,56,84)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:100048"
     Site            order(84,87,106,108..109,114,123,125..126,131..132,139,
                     141..142,144,148)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100048"
ORIGIN      
        1 mpelrdtgvr nvvcgenvvi yqpanlydcq lgdnvfvgpf veiqrntrig anskiqshtf
       61 iceyvtigqr cfighgvmfa ndlfregkpn adraswgrie igddvsigsg atilavsicd
      121 gvvigagsvv tksitekgvw agnparllrr l