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Information on EC 2.1.2.5 - glutamate formimidoyltransferase and Organism(s) Homo sapiens and UniProt Accession O95954

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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.
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This record set is specific for:
Homo sapiens
UNIPROT: O95954
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formiminoglutamic acid formiminotransferase
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-
-
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formiminoglutamic acid transferase
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-
-
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formiminoglutamic formiminotransferase
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-
-
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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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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formimino group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-83-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
show the reaction diagram
-
histidine degradation
-
?
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
show the reaction diagram
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
show the reaction diagram
-
-
-
r
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
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
show the reaction diagram
-
-
-
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
show the reaction diagram
-
histidine degradation
-
?
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
show the reaction diagram
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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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tetrahydrofolate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
free enzyme
Manually annotated by BRENDA team
reversibly associated with membrane, complex formation is increased by anti-liver cytosol type 1 autoantibodies
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme deficiency results in formiminoglutamic aciduria with elevated plasma and urine formiminoglutamic acid levels
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FTCD_HUMAN
541
0
58927
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C107R
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
subcellular localization of protein may influence production of autoantibodies and their role in the pathogenesis of type 2 autoimmune hepatitis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team