7.6.2.8: ABC-type vitamin B12 transporter
This is an abbreviated version!
For detailed information about ABC-type vitamin B12 transporter, go to the full flat file.
Word Map on EC 7.6.2.8
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7.6.2.8
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transcobalamin
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azurophilic
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cyanocobalamin
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lmbrd1
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outward-facing
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cobinamide
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inward-facing
- 7.6.2.8
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transcobalamin
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azurophilic
- cyanocobalamin
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lmbrd1
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outward-facing
- cobinamide
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inward-facing
Reaction
Synonyms
ABC transporter, ABCD4, BtuC, BtuCD, BtuCD vitamin B12 importer, BtuCD-BtuF, BtuCD-F, BtuCD-F complex, BtuD, BtuF, BtuF-CD, BtuM, BtuMTd, Cbl transporter, cobalamin-specific ECF-type ABC transporter, EC 3.6.3.33, ECF-CbrT, ECF-type ABC transporter for vitamin B12, energy coupling factor (ECF-) type ABC transporter, Rv1819c, Tbd_2719, vitamin B12 ABC importer, vitamin B12 import ATP-binding protein, vitamin B12 import system, vitamin B12 import system permease protein, vitamin B12 importer, vitamin B12 transporter, vitamin B12-binding protein, vitamin B12-transporting ATPase
ECTree
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Subunits
Subunits on EC 7.6.2.8 - ABC-type vitamin B12 transporter
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homodimer
additional information
additional information
crystal structure analysis for conformations of the transmembrane domains that form inner and outer gates, structure comparison, overview
additional information
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crystal structure analysis for conformations of the transmembrane domains that form inner and outer gates, structure comparison, overview
additional information
the homodimer BtuC spans the membrane and the two identical cytosolic ATPase domains BtuD form a sandwich dimer that couple chemical energy of two ATP molecules into structural changes of the full complex. A single substrate-binding protein (SBP) BtuF completes the transporter. BtuCD-F forms a stable complex in the ground state, analysis of crystal structures, PDB ID 2QI9 and 4DBL
additional information
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HI1470/1 shows intrinsic asymmetric conformational flexibility. The metal-chelate-type ABC transporter HI1470/1 is homologous with vitamin B12 importer BtuCD but exhibits a distinct inward-facing conformation in contrast to the outward-facing conformation of BtuCD. The outward-facing conformation of HI1470/1 is considered to be one of the intermediate states in the translocation cycle of BtuCD
additional information
the regions around transmembrane domains (TMs) 2, 5 and 3 are critical for the correct dimerization of ABCD4
additional information
ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family
additional information
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ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family
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additional information
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ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family
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additional information
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ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family
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additional information
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ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family
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additional information
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ECF-transporters are multi-subunit membrane complexes that consist of two ATPases, similar to the ATPases of ABC transporters, and two membrane embedded proteins, not related to any other protein family
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additional information
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ABC-transporter