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Information on EC 7.6.2.9 - ABC-type quaternary amine transporter

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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 quaternary amine derivatives.
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This record set is specific for:
UNIPROT: O32243
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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quaternary amine-[quaternary amine-binding protein][side 1]
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quaternary amine[side 2]
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[quaternary amine-binding protein][side 1]
Synonyms
abc transporter, opuac, glycine betaine-binding protein, opubc, opucc, glycine betaine porter ii, opuab, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycine betaine/carnitine/choline-binding protein
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Quaternary-amine-transporting ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, quaternary-amine-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 quaternary amine derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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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?
OPUCC_BACSU
Bacillus subtilis (strain 168)
303
0
33957
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
substrate-binding protein OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine to 2.3, 2.7, 2.4, 1.9 and 2.1 A resolution, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with a substrate-binding pocket located at the interdomain cleft. Upon substrate binding, the two domains shift towards each other to trap the substrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T94D
shares a quite similar pattern of fluorescence spectrum to that of the paralogue OpuBC. Only choline can trigger obvious changes of fluorescence intensity of mutant T94D, whereas carnitine, GB and ectoine cannot
Y91A
complete loss of binding affinity
Y91F
slight decrease in binding affinity
Y91W
slight decrease in binding affinity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Du, Y.; Shi, W.W.; He, Y.X.; Yang, Y.H.; Zhou, C.Z.; Chen, Y.
Structures of the substrate-binding protein provide insights into the multiple compatible solute binding specificities of the Bacillus subtilis ABC transporter OpuC
Biochem. J.
436
283-289
2011
Bacillus subtilis (O32243), Bacillus subtilis
Manually annotated by BRENDA team