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Information on EC 7.6.2.8 - ABC-type vitamin B12 transporter

for references in articles please use BRENDA:EC7.6.2.8
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EC Tree
IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of cobalamin derivatives.
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This record set is specific for:
UNIPROT: P37028
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
btucd, abcd4, vitamin b12-binding protein, btucd-f, vitamin b12 transporter, rv1819c, vitamin b12 importer, btucd-btuf, btucd-f complex, ecf-cbrt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
vitamin B12 transporter
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vitamin B12-transporting ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, vitamin B12-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of cobalamin derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + vitamin B12/out
ADP + phosphate + vitamin B12/in
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + vitamin B12/out
ADP + phosphate + vitamin B12/in
show the reaction diagram
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BTUF_ECOLI
Escherichia coli (strain K12)
266
0
29367
Swiss-Prot
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, M.; Sun, T.; Hu, J.; Chen, W.; Wang, C.
Study on the mechanism of the BtuF periplasmic-binding protein for vitamin B(12)
Biophys. Chem.
135
19-24
2008
Escherichia coli (P37028)
Manually annotated by BRENDA team
Sonne, J.; Kandt, C.; Peters, G.H.; Hansen, F.Y.; Jensen, M.?.; Tieleman, D.P.
Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD
Biophys. J.
92
2727-2734
2007
Escherichia coli (P37028)
Manually annotated by BRENDA team
Su, J.G.; Zhang, X.; Zhao, S.X.; Li, X.Y.; Hou, Y.X.; Wu, Y.D.; Zhu, J.Z.; An, H.L.
Conformational motions and functionally key residues for vitamin B12 transporter BtuCD-BtuF revealed by elastic network model with a function-related internal coordinate
Int. J. Mol. Sci.
16
17933-17951
2015
Escherichia coli (P37028), Escherichia coli
Manually annotated by BRENDA team