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EC Tree
IUBMB Comments The enzyme also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate. In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
The taxonomic range for the selected organisms is: Homo sapiens The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
formiminotransferase-cyclodeaminase, glutamate formiminotransferase, glutamate formyltransferase, formiminoglutamic acid formiminotransferase,
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formiminoglutamic acid formiminotransferase
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formiminoglutamic acid transferase
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formiminoglutamic formiminotransferase
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formiminotransferase cyclodeaminase
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formiminotransferase, glutamate
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formiminotransferase-cyclodeaminase
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glutamate formiminotransferase
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glutamate formyltransferase
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FTCD
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formimino group transfer
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5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
The enzyme also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate. In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
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5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
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N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine degradation
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tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
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r
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
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tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
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5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
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N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine degradation
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tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
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Anemia, Megaloblastic
Congenital errors of folate metabolism.
glutamate formimidoyltransferase deficiency
Characteristics and outcomes of patients with formiminoglutamic aciduria detected through newborn screening.
glutamate formimidoyltransferase deficiency
Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency.
glutamate formimidoyltransferase deficiency
Congenital errors of folate metabolism.
glutamate formimidoyltransferase deficiency
Falsely elevated C4-carnitine as expression of glutamate formiminotransferase deficiency in tandem mass spectrometry newborn screening.
glutamate formimidoyltransferase deficiency
Formiminoglutamic aciduria in a slightly retarded boy with chronic obstructive lung disease.
glutamate formimidoyltransferase deficiency
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer.
glutamate formimidoyltransferase deficiency
The molecular basis of glutamate formiminotransferase deficiency.
glutamate formimidoyltransferase deficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
Hepatitis, Autoimmune
Characterization of the antigenicity of the formiminotransferase-cyclodeaminase in type 2 autoimmune hepatitis.
Hepatitis, Autoimmune
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer.
Malnutrition
Resistance of liver formiminoglutamic acid transferase to experimental protein malnutrition in weanling rats.
methionine synthase deficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
methylenetetrahydrofolate dehydrogenase (nad+) deficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
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additional information
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UniProt
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free enzyme
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reversibly associated with membrane, complex formation is increased by anti-liver cytosol type 1 autoantibodies
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more abundantly around the mother centriole. The centrosome localization of FTCD continues throughout the cell cycle and is not disrupted after Golgi fragmentation, which is induced by colcemid and brefeldin A. FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
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additional information
no interaction of enzyme with liver-specific cytoskeleton proteins
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additional information
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no interaction of enzyme with liver-specific cytoskeleton proteins
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malfunction
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enzyme deficiency results in formiminoglutamic aciduria with elevated plasma and urine formiminoglutamic acid levels
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FTCD_HUMAN
541
0
58927
Swiss-Prot
other Location (Reliability: 2 )
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C107R
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the mutation causes formiminoglutamic aciduria
D89G
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the mutation causes formiminoglutamic aciduria
E456G
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the mutation causes formiminoglutamic aciduria
G144R
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the mutation causes formiminoglutamic aciduria
G172W
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the mutation causes formiminoglutamic aciduria
K151*
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the mutation causes formiminoglutamic aciduria
L536*
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the mutation causes formiminoglutamic aciduria
M75L
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the mutation causes formiminoglutamic aciduria
Q113*
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the mutation causes formiminoglutamic aciduria
R135C
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mutation naturally occuring in patient with mild form of putative glutamate formiminotransferase deficiency
R255*
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the mutation causes formiminoglutamic aciduria
R299P
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mutation naturally occuring in patient with mild form of putative glutamate formiminotransferase deficiency
V458del
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the mutation causes formiminoglutamic aciduria
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medicine
subcellular localization of protein may influence production of autoantibodies and their role in the pathogenesis of type 2 autoimmune hepatitis
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Tabor, H.; Wyngarden, L.
The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid
J. Biol. Chem.
234
1830-1846
1959
Bos taurus, Cavia porcellus, Felis catus, Homo sapiens, Mus musculus, Oryctolagus cuniculus, Sus scrofa
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Renous, R.; Lapierre, P.; Djilali-Saiah, I.; Vitozzi, S.; Alvarez, F.
Characterization of the antigenicity of the formiminotransferase-cyclodeaminase in type 2 autoimmune hepatitis
Exp. Cell Res.
292
332-341
2004
Homo sapiens (O95954), Homo sapiens
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Hilton, J.F.; Christensen, K.E.; Watkins, D.; Raby, B.A.; Renaud, Y.; de la Luna, S.; Estivill, X.; MacKenzie, R.E.; Hudson, T.J.; Rosenblatt, D.S.
The molecular basis of glutamate formiminotransferase deficiency
Hum. Mutat.
22
67-73
2003
Homo sapiens, Sus scrofa
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Hagiwara, H.; Tajika, Y.; Matsuzaki, T.; Suzuki, T.; Aoki, T.; Takata, K.
Localization of Golgi 58K protein (formiminotransferase cyclodeaminase) to the centrosome
Histochem. Cell Biol.
126
251-259
2006
Homo sapiens (O05954)
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Majumdar, R.; Yori, A.; Rush, P.W.; Raymond, K.; Gavrilov, D.; Tortorelli, S.; Matern, D.; Rinaldo, P.; Feldman, G.L.; Oglesbee, D.
Allelic spectrum of formiminotransferase-cyclodeaminase gene variants in individuals with formiminoglutamic aciduria
Mol. Genet. Genomic Med.
5
795-799
2017
Homo sapiens
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