D,D-heptose 7-phosphate kinase
InterPro Protein Domain record
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description
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<p>This group of enzymes belongs to the GHMP kinase domain superfamily. GHMP kinases are a unique class of ATP-dependent enzymes (the abbreviation of which refers to the original members: galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) [<cite idref="PUB00015675"/>]. Enzymes belonging to this superfamily contain three well-conserved motifs, the second of which has the typical sequence Pro-X-X-X-Gly-Leu-X-Ser-Ser-Ala and is involved in ATP binding [<cite idref="PUB00015644"/>]. The phosphate binding loop in GHMP kinases is distinct from the classical P-loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P-loop-containing proteins [<cite idref="PUB00015644"/>]. GHMP kinases display a distinctly bilobal appearance with their N-terminal subdomains dominated by a mixed beta-sheet flanked on one side by alpha-helices and their C-terminal subdomains containing a four stranded anti-parallel beta-sheet [<cite idref="PUB00015835"/>, <cite idref="PUB00015644"/>, <cite idref="PUB00015669"/>, <cite idref="PUB00015730"/>].</p> <p> <taxon tax_id="143495">Aneurinibacillus thermoaerophilus</taxon> protein has been characterised as a D-glycero-D-manno-heptose 7-phosphate kinase that adds phosphate group to C-1 of D-glycero-D-manno-heptose 7-phosphate [<cite idref="PUB00016208"/>], and has been called GmhB or HddA. Note that HddA is the preferred name for this protein because the name GmhB has also been used for the D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase, <db_xref db="PIRSF" dbkey="PIRSF004682"/> [<cite idref="PUB00015918"/>, <cite idref="PUB00015950"/>]. This enzyme catalyses a step in the biosynthesis of the nucleotide-activated form GDP-D-glycero-D-manno-heptose [<cite idref="PUB00016208"/>] and is encoded by the heptose operon [<cite idref="PUB00016208"/>].</p> <p>D-glycero-D-manno-heptose is a constituent of lipopolysaccharide (LPS) cores of Gram-negative bacteria, and also a component of the S-layer glycoprotein of the Gram-positive bacterium <taxon tax_id="143495">Aneurinibacillus thermoaerophilus</taxon>. The principal architecture of S-layer glycoproteins resembles that of the LPS of Gram-negative bacteria and comparable pathways are used for the biosynthesis of these similar glycoconjugates [<cite idref="PUB00016208"/>].</p> <p>WcbL of <taxon tax_id="28450">Burkholderia pseudomallei</taxon> is also involved in the synthesis of an LPS (type I O-polysaccharide moieties) [<cite idref="PUB00015917"/>].</p> <p>LmbP is thought to belong to the lincomycin-production gene cluster of <taxon tax_id="1915">Streptomyces lincolnensis</taxon> [<cite idref="PUB00003870"/>].</p>
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D,D-heptose 7-phosphate kinase
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InterPro Protein Domain record
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