L-lactate dehydrogenase [Listeria monocytogenes].

LOCUS       WP_009932004             302 aa            linear   BCT 28-FEB-2022
ACCESSION   WP_009932004
VERSION     WP_009932004.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 302)
  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 302)
  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..302
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..302
                     /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=32321
     Region          3..300
                     /region_name="HicDH_like"
                     /note="L-2-hydroxyisocapronate dehydrogenases and some
                     bacterial L-lactate dehydrogenases; cd05291"
                     /db_xref="CDD:133427"
     Site            order(3,28,57,161,163,166,185,190..191,241..245,247,269,
                     277..278)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133427"
     Site            order(11..13,34..35,77..80,118..120,143,175)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133427"
     Site            order(15..16,19,23..24,43,45..49,52..53,150..151,153,165,
                     221..222,226..228,231,235)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133427"
     Site            order(88,120,151,175,215,225)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133427"
ORIGIN      
        1 mkrkvgiigt ghvgsdvafs lvtqgicdei vlidkietka esealelrdm asmtnsytmi
       61 tsndwsalgd advivmavgp etllredrme elvetsrsva eivpkiiasg fqgifvnitn
      121 pcdvitmliq klsgfdhsrv fgtgtsldta rmrrvvgeal hinpksvegy vlgehgesqf
      181 vawstvkigg vsikdykttt sldlpalkda vrgggwnilt gkgwtsfgia tavagivdai
      241 ltdakqvfpl avfsektsty igqpaligan gvidileppl tetekinfne saeiiknafq
      301 li