MULTISPECIES: L-lactate dehydrogenase [Klebsiella].

LOCUS       WP_002904491             314 aa            linear   BCT 28-FEB-2022
ACCESSION   WP_002904491
VERSION     WP_002904491.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Jonsson,M., Saleihan,Z., Nes,I.F. and Holo,H.
  TITLE     Construction and characterization of three lactate
            dehydrogenase-negative Enterococcus faecalis V583 mutants
  JOURNAL   Appl Environ Microbiol 75 (14), 4901-4903 (2009)
   PUBMED   19465534
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Hannenhalli,S.S. and Russell,R.B.
  TITLE     Analysis and prediction of functional sub-types from protein
            sequence alignments
  JOURNAL   J Mol Biol 303 (1), 61-76 (2000)
   PUBMED   11021970
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 :: TIGR01771.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..314
                     /product="L-lactate dehydrogenase"
                     /EC_number="1.1.1.27"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004459 - L-lactate dehydrogenase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=33268
     Region          6..312
                     /region_name="HicDH_like"
                     /note="L-2-hydroxyisocapronate dehydrogenases and some
                     bacterial L-lactate dehydrogenases; cd05291"
                     /db_xref="CDD:133427"
     Site            order(6,31,60,165,167,170,189,194..195,248..252,254,280,
                     288..289)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133427"
     Site            order(14..16,37..38,80..81,83..84,122..124,147,179)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133427"
     Site            order(18..19,22,26..27,46,48..52,55..56,154..155,157,169,
                     228..229,233..235,238,242)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133427"
     Site            order(92,124,155,179,222,232)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133427"
ORIGIN      
        1 mhtkarkvmi igagnvgasa ayallnqsic eelilvdlnq qraeahaqdl sdaaaylpgm
       61 mtistreasd cadvdiavit vsggalrpgq srldeltsta kivksivptm mangfngifl
      121 vatnpcdiit wqvwqlsglp rsqvlgtgvw ldttrlrrll aqeleigaqs idafilgehg
      181 dtqfpvwshs svygtpiadl yqqrtglpld reamadkvrk lgfeiyagkg cteygvagti
      241 aeicrniftg shralavsci ldgeygvsga aagvpavlaq ggvkqiielq lageeqakfs
      301 qsiavikani arlp