LOCUS       WP_011185979             488 aa            linear   BCT 28-FEB-2022
DEFINITION  pyruvate kinase [Leifsonia xyli].
ACCESSION   WP_011185979
VERSION     WP_011185979.1
KEYWORDS    RefSeq.
SOURCE      Leifsonia xyli
  ORGANISM  Leifsonia xyli
            Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
            Microbacteriaceae; Leifsonia.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Eijkel,J.C. and van den Berg,A.
  TITLE     Nanofluidics and the chemical potential applied to solvent and
            solute transport
  JOURNAL   Chem Soc Rev 39 (3), 957-973 (2010)
   PUBMED   20179818
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 :: TIGR01064.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Leifsonia xyli"
                     /db_xref="taxon:1575"
     gene            1..488
                     /gene="pyk"
     Protein         1..488
                     /product="pyruvate kinase"
                     /EC_number="2.7.1.40"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004743 - pyruvate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006096 - glycolytic process [Evidence
                     IEA]"
                     /calculated_mol_wt=52309
     Region          2..468
                     /region_name="Pyruvate_Kinase"
                     /note="Pyruvate kinase (PK): Large allosteric enzyme that
                     regulates glycolysis through binding of the substrate,
                     phosphoenolpyruvate, and one or more allosteric effectors.
                     Like other allosteric enzymes, PK has a high substrate
                     affinity R state and a low...; cl39076"
                     /db_xref="CDD:453956"
     Site            order(3..4,60,62,70..73,156..157,163,166..170,185,193,200,
                     211,247,265..266,270,302,304,333,385,387,389,400,403..404,
                     406,408..410)
                     /site_type="active"
                     /note="domain interfaces [active]"
                     /db_xref="CDD:238178"
     Site            order(32,34,66,191,217,219,243,275)
                     /site_type="active"
                     /db_xref="CDD:238178"
ORIGIN      
        1 mrrakivatl gpatssydni raivdagvdv armnlshgsy evhegvyanv rkaaedagkp
       61 vavlvdlqgp kirlgkfeag pyelaegdif titteeiigt keissttfkg lpqdvkpgdf
      121 lliddgkvrv rvletdgtav ttevvvagpv snnkginlpg vavnvpalse kdeadlrwgl
      181 nlgadlials fvrnagdier vheimaeegr kvpviakiek pqavdalegi ieafdgimva
      241 rgdlgvelpl eavpivqkra velarraakp vivatqmles misspvptra etsdvanavl
      301 dgsdavmlsg etsvgeypki tvqtmakivk steehgldri aplgtkprtq sgaitlaate
      361 vadfveakyl cvftesgesa rrmarlrski rilaftpees trrkmalywg vesfvvdrvt
      421 htdqmvaqvd ealkstgrae ngdkvviisg sppgipgttn dirvhrvgdv lcsetqrras
      481 rfgdrsrl
//