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Information on EC 6.3.2.B3 - tubulin-glutamate ligase
for references in articles please use BRENDA:EC6.3.2.B3
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Old data from external sources may still be available.
Please check here for current data: EC 6.3.2.61
Please check here for current data: EC 6.3.2.61
deleted, replaced by EC 6.3.2.61, tubulin-glutamate ligase
Synonyms
alpha-tubulin polyglutamylase, TTHERM_00773080, TTL domain protein, TTLL1, TTLL9, tubulin glutamylase, tubulin tyrosine ligase domain protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-tubulin polyglutamylase
TTHERM_00773080
TTL domain protein
TTLL1
TTLL9
tubulin glutamylase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + alpha-tubulin + L-glutamate
L-glutamyl-alpha-tubulin + ADP + phosphate
Substrates: -
Products: -
Products: -
?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
main localization, GFP-tagged recombinant protein
brenda
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main localization, GFP-tagged recombinant protein
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brenda
Ttll1 localizes primarily to the basal bodies of oral and somatic cilia
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brenda
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Ttll1 localizes primarily to the basal bodies of oral and somatic cilia
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Ttll9 glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
physiological function
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
physiological function
-
Ttll9 glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
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physiological function
-
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). I7MCG4_TETTS
Tetrahymena thermophila (strain SB210)
648
0
75425
TrEMBL
-
TTLL1_TETTS
Tetrahymena thermophila (strain SB210)
413
0
48267
Swiss-Prot
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of recombinant GFP-tagged Ttll1 and GFP-tagged Ttll9
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of GFP-tagged protein in Tetrahymena thermophila
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wloga, D.; Rogowski, K.; Sharma, N.; van Dijk, J.; Janke, C.; Edde, B.; Bre, M.-H.; Levilliers, N.; Redeker, V.; Duan, J.; Gorovsky, M.A.; Jerka-Dziadosz, M.; Gaertig, J.
Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila
Eukaryot. Cell
7
1362-1372
2008
Tetrahymena thermophila (Q23SI8), Tetrahymena thermophila (I7MCG4), Tetrahymena thermophila SB210 (I7MCG4), Tetrahymena thermophila SB210 (Q23SI8)
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brenda
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