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Information on EC 5.6.1.3 - plus-end-directed kinesin ATPase

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EC Tree
IUBMB Comments
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
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UNIPROT: Q383K3
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
kinesin, kinesin-1, kif3a, kinesin-5, kif1a, kif11, kif4a, kifc1, kinesin-2, kif5b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
orphan kinesin
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kinesin
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
kinesin ATP phosphohydrolase (plus-end-directed)
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
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 + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
show the reaction diagram
additional information
?
-
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 + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Tb927.11.10760
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
orphan kinesin TbKIN-D associates with cytoskeletal microtubules and is distributed throughout the cytoskeleton at all cell cycle stages
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
depletion of TbKIN-D disrupts cell morphology, resulting in elongation of the posterior of the cell, which is filled with newly assembled microtubules. RNAi of TbKIN-D impairs organelle segregation and leads to severe growth inhibition and cell death, TbKIN-D deficiency significantly interferes with cytoskeletal microtubules, phenotype
physiological function
microtubules are a vital part of the cytoskeleton of eukaryotic cells and are involved in various cellular processes. The cytoskeleton of Trypanosoma brucei is characterized by an array of subpellicular microtubules and is essential for maintenance of cell shape and polarity, the orphan kinesin TbKIN-D in trypanosomes cooperates with a kinetoplastid-specific kinesin to maintain cell morphology by regulating subpellicular microtubules. The orphan kinesin TbKIN-D regulates the organization of subpellicular microtubules and is required for maintaining cell morphology, and TbKIN-D possesses in vitro ATPase activity and associates with cytoskeletal microtubules. Enzyme TbKIN-D is essential for cell proliferation and viability
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q383K3_TRYB2
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
617
0
69885
TrEMBL
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of orphan kinesin TbKIN-D and kinetoplastid-specific kinesin TbKIN-C by tandem affinity purification in a two-step chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Tb927.11.10760
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hu, H.; Hu, L.; Yu, Z.; Chasse, A.E.; Chu, F.; Li, Z.
An orphan kinesin in trypanosomes cooperates with a kinetoplastid-specific kinesin to maintain cell morphology by regulating subpellicular microtubules
J. Cell Sci.
125
4126-4136
2012
Trypanosoma brucei (Q383K3), Trypanosoma brucei
Manually annotated by BRENDA team