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Literature summary for 7.6.2.10 extracted from

  • D'Rozario, R.S.; Sansom, M.S.
    Helix dynamics in a membrane transport protein: comparative simulations of the glycerol-3-phosphate transporter and its constituent helices (2008), Mol. Membr. Biol., 25, 571-583.
    View publication on PubMed
Search for more literature for 7.6.2.10

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the enzyme contains 12-transmembrane alpha-helices which form two domains, each of six transmembrane helices, surrounding a central lingand-binding cavity Escherichia coli 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli GltP is an organic phosphate/inorganic phosphate antiporter ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information GltP is an organic phosphate/inorganic phosphate antiporter Escherichia coli ?
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 ?

Subunits

Subunits Comment Organism
More the enzyme contains 12 highly flexible transmembrane alpha-helices, H1-H12, which form two domains, each of six transmembrane helices, surrounding a central lingand-binding cavity, molecular dynamic simulations and modelling, comparison of conformational properties with other MFS family members, overview Escherichia coli

Synonyms

Synonyms Comment Organism
GltP
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 Escherichia coli
glycerol-3-phosphate transporter
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 Escherichia coli
More the enzyme belongs to the major facilitator MFS transporter superfamily Escherichia coli