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Literature summary for 7.6.2.5 extracted from
- Structural basis for heme recognition by HmuT responsible for heme transport to the heme transporter in Corynebacterium glutamicum (2016), Chem. Lett., 45, 24-26 .
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene hmuT, lactose-inducible recombinant expression of His-tagged HmuT in Escherichia coli strain BL21(DE3) | Corynebacterium glutamicum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant His-tagged purified CgHmuT from enzyme complex HmuTUV in the holo-form, hanging drop vapour diffusion method, mixing of 50 mg/ml protein in 50 mM Tris-HCl, pH 8.5, and 200 mM NaCl with precipitant solution containing 2.1 M ammonium sulfate and 0.2 M potassium thiocyanate, X-ray diffraction structure determination and analysis at 1.42 A resolution | Corynebacterium glutamicum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| inner membrane | periplasmic heme-binding protein HmuT binds heme to transport it to an ABC-type heme transporter, which transports it through the inner membrane to the cytoplasm | Corynebacterium glutamicum | - |
- |
| periplasm | periplasmic heme-binding protein HmuT binds heme to transport it to an ABC-type heme transporter | Corynebacterium glutamicum | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Corynebacterium glutamicum |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + heme[side 1] | Corynebacterium glutamicum | - |
ADP + phosphate + heme[side 2] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | A0A160PR71 AND A0A160PQ30 AND A0A169RPR0 | ABC-type heme transporter system HmuTUV encoded by genes hmut, hmuu, and hmuv | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged HmuT from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, followed by gel filtration and unltrafiltration, HmuT is obtained in holo-form | Corynebacterium glutamicum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + heme[side 1] | - |
Corynebacterium glutamicum | ADP + phosphate + heme[side 2] | - |
? | |
| additional information | there is a cleft between the N- and C-terminal domains, in which one heme molecule is accommodated with His141 and Tyr240 as axial ligands that are located at the loop regions in the N- and C-terminal domains, respectively. The Fe-N and Fe-O bond distances are 2.2 and 2.1 A, respectively. Heme is accommodated in the heme-binding site of CgHmuT with two different orientations | Corynebacterium glutamicum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | there is a cleft between the N- and C-terminal domains, in which one heme molecule is accommodated with His141 and Tyr240 as axial ligands that are located at the loop regions in the N- and C-terminal domains, respectively. The Fe-N and Fe-O bond distances are 2.2 and 2.1 A, respectively. Heme-binding protein structure comparisons, overview | Corynebacterium glutamicum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ABC-type heme transporter | - |
Corynebacterium glutamicum |
| CgHmuT | - |
Corynebacterium glutamicum |
| HmuT | - |
Corynebacterium glutamicum |
| HmuTUV | - |
Corynebacterium glutamicum |
| HmuU | - |
Corynebacterium glutamicum |
| HmuV | - |
Corynebacterium glutamicum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Corynebacterium glutamicum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | substrate heme is accommodated with two different orientations in the central cleft of the HmuTUV complex protein CgHmuT, in which His141 and Tyr240 are coordinated to the heme as axial ligands | Corynebacterium glutamicum |
| physiological function | HmuT from Corynebacterium glutamicum is a heme-binding protein in an ABC-type heme transporter system, HmuTUV. The Corynebacterium glutamicum heme acquisition system consists of HtaA, HtaB, and HmuTUV. Heme is transported into the cytoplasm by this ABC transporter. Heme is captured by the membrane-anchored heme-binding proteins, HtaA and HtaB, and is transferred to HmuT, which is a heme-binding protein for the ABC-type heme transporter HmuUV. Pathogenic bacteria use heme as an iron source partly because heme is the most abundant iron species in their host | Corynebacterium glutamicum |
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