Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

The annotation and conditions in this rule are derived from the following entries: P0CW93 (LDH2_BIFLO), P00344 (LDH_GEOSE), P00343 (LDH_LACCA), O32765 (LDH_LACHE), P16115 (LDH_THEMA)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00488
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 157 - 157 aligns to "[RK]" in entry P00344 Subsequence at position 172 - 172 aligns to "H" in entry P00344
    • Subsequence at position 223 - 223 aligns to "Y" in entry P13714
    • scientific organism = Staphylococcus aureus
    • Subsequence at position 17 - 17 aligns to "V" in entry P00344 (individually applies "NAD; via amide nitrogen")
    • Subsequence at position 38 - 38 aligns to "[DNE]" in entry P00344 (individually applies "NAD")
    • Subsequence at position 43 - 43 aligns to "[RK]" in entry P00344 (individually applies "NAD")
    • Subsequence at position 69 - 69 aligns to "Y" in entry P00344 (individually applies "NAD")
    • Subsequence at position 83 - 84 aligns to "G-[AVL]" in entry P00344 (individually applies "NAD")
    • Subsequence at position 86 - 86 aligns to "Q" in entry P00344 (individually applies "Substrate")
    • Subsequence at position 92 - 92 aligns to "R" in entry P00344 (individually applies "Substrate")
    • Subsequence at position 105 - 105 aligns to "[ST]" in entry P00344 (individually applies "NAD")
    • Subsequence at position 122 - 124 aligns to "[AIV]-x-N" in entry P00344 (individually applies "NAD")
    • Subsequence at position 124 - 127 aligns to "N-x-x-D" in entry P00344 (individually applies "Substrate binding")
    • Subsequence at position 147 - 147 aligns to "[ST]" in entry P00344 (individually applies "NAD")
    • Subsequence at position 152 - 155 aligns to "D-x-x-R" in entry P00344 (individually applies "Substrate binding")
    • Subsequence at position 179 - 179 aligns to "H" in entry P00344 (individually applies "Proton acceptor")
    • Subsequence at position 233 - 233 aligns to "T" in entry P00344 (individually applies "Substrate")
  • Subsequence at position 157 - 157 aligns to "[RK]" in entry P00344 (applies "Allosteric activator") Subsequence at position 172 - 172 aligns to "H" in entry P00344 (applies "Allosteric activator")
    • Subsequence at position 223 - 223 aligns to "Y" in entry P13714

... then these annotations are applied i

Protein namei

  • Recommended name:
    L-lactate dehydrogenase (EC:1.1.1.27)
    Short name:
    L-LDH

Gene namei

  • Name:ldh

Activity regulationi

  • Allosterically activated by fructose 1,6-bisphosphate (FBP).

Subunit structurei

  • Homotetramer.

Functioni

  • Catalyzes the conversion of lactate to pyruvate.

Sequence similaritiesi

Pathwayi

  • Pathwayi: pyruvate fermentation to lactate

    This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate. This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Subcellular locationi

Catalytic activityi

  • (S)-lactate + NAD+ = pyruvate + NADH.

Regioni

  • Substrate binding (to residues corresponding to positions 124 - 127)
  • Substrate binding (to residues corresponding to positions 152 - 155)

Binding sitei

  • NAD; via amide nitrogen (to residues corresponding to position 17)
  • NAD (to residues corresponding to position 38)
  • NAD (to residues corresponding to position 43)
  • NAD (to residues corresponding to position 69)
  • Substrate (to residues corresponding to position 86)
  • Substrate (to residues corresponding to position 92)
  • NAD (to residues corresponding to position 105)
  • NAD (to residues corresponding to position 147)
  • Substrate (to residues corresponding to position 233)
  • Allosteric activator (to residues corresponding to position 157)
  • Allosteric activator (to residues corresponding to position 172)

Modified residuei

  • Phosphotyrosine (to residues corresponding to position 223)

Nucleotide bindingi

  • NAD (to residues corresponding to positions 83 - 84)
  • NAD (to residues corresponding to positions 122 - 124)

Active sitei

  • Proton acceptor (to residues corresponding to position 179)

Keywordsi

GO (Gene Ontology) termsi

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again