L-lactate dehydrogenase [Listeria monocytogenes].

LOCUS       WP_003732587             311 aa            linear   BCT 11-APR-2024
ACCESSION   WP_003732587
VERSION     WP_003732587.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 311)
  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 311)
  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..311
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..311
                     /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=33610
     Region          4..310
                     /region_name="HicDH_like"
                     /note="L-2-hydroxyisocapronate dehydrogenases and some
                     bacterial L-lactate dehydrogenases; cd05291"
                     /db_xref="CDD:133427"
     Site            order(4,29,58,163,165,168,187,192..193,246..250,252,278,
                     286..287)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133427"
     Site            order(12..14,35..36,78..81,120..122,145,177)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133427"
     Site            order(16..17,20,24..25,44,46..50,53..54,152..153,155,167,
                     226..227,231..233,236,240)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133427"
     Site            order(90,122,153,177,220,230)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133427"
ORIGIN      
        1 mkprkvmiig agnvgtaaah afvnqkfvee lilvdlnker vegnrkdlad aaafmpgkmd
       61 itvrdasdca dvdiavitvt agplkegqtr ldelrstsri vsgivpemmk ggfngiflia
      121 tnpcdiityq vwklsglpre rvlgtgvwld ttrlrrllae kldiaaqsid afilgehgds
      181 qfpvwshssi ygkpvneysl eklgesldlk qigetardtg feiyhqkgct eygiggtive
      241 icrhifsgsq raltvscvld geygesglai gvpavlsqng vkeiislkld eqeqqafans
      301 vsvikksias i