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Information on EC 7.5.2.8 - ABC-type D-allose transporter

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EC Tree
IUBMB Comments
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-allose, which can be used by the bacterium as a sole carbon source.
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This record set is specific for:
UNIPROT: P39265
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The expected taxonomic range for this enzyme is: Escherichia coli
Reaction Schemes
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D-allose-[allose-binding protein][side 1]
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[allose-binding protein][side 1]
Synonyms
allose binding protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
allose binding protein
subunit of the D-allose transport system
alsBAC
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D-allose ABC transporter
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D-allose transporting ATPase
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, D-allose-importing)
ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-allose, which can be used by the bacterium as a sole carbon source.
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 + D-allose-[allose-binding protein][side 1]
ADP + phosphate + D-allose[side 2] + [allose-binding protein][side 1]
show the reaction diagram
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?
additional information
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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 + D-allose-[allose-binding protein][side 1]
ADP + phosphate + D-allose[side 2] + [allose-binding protein][side 1]
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
contains zinc
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALSB_ECOLI
Escherichia coli (strain K12)
311
0
32910
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
D-allose binding protein bound to D-allose, hanging drop vapor diffusion method, using 40-60% (w/v) monomethyl polyethyleneglycol 550, 0.01 M zinc sulfate, and 0.1 M Mes buffer at pH 6.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chaudhuri, B.N.; Ko, J.; Park, C.; Jones, T.A.; Mowbray, S.L.
Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution
J. Mol. Biol.
286
1519-1531
1999
Escherichia coli (P39265), Escherichia coli
Manually annotated by BRENDA team