MULTISPECIES: isocitrate lyase/PEP mutase family protein

LOCUS       WP_004152903             248 aa            linear   BCT 20-JAN-2025
            [Klebsiella].
ACCESSION   WP_004152903
VERSION     WP_004152903.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Narayanan,B.C., Niu,W., Han,Y., Zou,J., Mariano,P.S.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and function of PA4872 from Pseudomonas aeruginosa, a
            novel class of oxaloacetate decarboxylase from the PEP
            mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 47 (1), 167-182 (2008)
   PUBMED   18081320
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Chen,C.C., Han,Y., Niu,W., Kulakova,A.N., Howard,A., Quinn,J.P.,
            Dunaway-Mariano,D. and Herzberg,O.
  TITLE     Structure and kinetics of phosphonopyruvate hydrolase from
            Variovorax sp. Pal2: new insight into the divergence of catalysis
            within the PEP mutase/isocitrate lyase superfamily
  JOURNAL   Biochemistry 45 (38), 11491-11504 (2006)
   PUBMED   16981709
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 10616714
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..248
                     /product="isocitrate lyase/PEP mutase family protein"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=27008
     Region          3..238
                     /region_name="PEP_mutase"
                     /note="Phosphoenolpyruvate phosphomutase; pfam13714"
                     /db_xref="CDD:433424"
ORIGIN      
        1 mdfnalhqqn qplllanvwd assaqaaqqa gyqalgsssa aiaamlgyed geemsfdelf
       61 yvvsriktvs elplsvdlea gygattshii dnirrlahlg vsginledsh vvdgtrrldd
      121 aerfavklqe itracpglfv nvrtdtflln vqdalvqtly rgqlyakhga cgffvpcvtr
      181 aeditaivhh vplplnvmcm peladfstls tlgvkrismg nfiyaatqar lkdllcqvqt
      241 qhsfsgvf