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Information on EC 2.1.2.5 - glutamate formimidoyltransferase and Organism(s) Rattus norvegicus and UniProt Accession O88618
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2.1.2.5 glutamate formimidoyltransferaseIUBMB 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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Word Map
- 2.1.2.5
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octameric
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megaloblastic
-
aciduria
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formylation
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folinic
- polyglutamate
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figlu
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monofunctional
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polyglutamylated
- methylenetetrahydrofolate
- histidase
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
formiminotransferase-cyclodeaminase, glutamate formiminotransferase, glutamate formyltransferase, formiminoglutamic acid formiminotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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, glutamate
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-
-
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glutamate formiminotransferase
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-
-
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glutamate formyltransferase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formimino group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
9032-83-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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metabolic enzyme involved in the conversion of histidine to glutamic acid
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine metabolism pathway, reaction occurs in vivo within the soluble phase of cytoplasm
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?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
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-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
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transfer of a single carbon from formiminoglutamate to tetrahydrofolate, product is 5-formiminotetrahydrofolate
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?
additional information
?
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58K: formiminotransferase cyclodeaminase, bifunctional enzyme catalyzing two consecutive steps in the modification of tetrahydrofolate to 5,10-methenyl tetrahydrofolate
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-
?
additional information
?
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58K: formiminotransferase cyclodeaminase, bifunctional enzyme catalyzing two consecutive steps in the modification of tetrahydrofolate to 5,10-methenyl tetrahydrofolate
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
metabolic enzyme involved in the conversion of histidine to glutamic acid
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine metabolism pathway, reaction occurs in vivo within the soluble phase of cytoplasm
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
proteinase K
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degradation of bifunctional formiminotransferase cyclodeaminase
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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richest tissue source of formiminotransferase cyclodeaminase, liver-specific enzyme
additional information
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no activity in the soluble proteins of brain, heart, lung, testis, intestinal mucosa, diaphragm muscle or spleen
additional information
-
undetectable in adrenal gland, blood cells, marrow cells, brain, epididymis, heart, small intestine, kidney, lung, skeletal muscle, spleen and testis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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formiminotransferase cyclodeaminase binds bovine brain microtubules, but not rat liver microtubules in vitro
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formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmic surface of the Golgi apparatus in vivo, cytoplasmically oriented peripheral membrane protein of the Golgi membranes
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formiminotransferase cyclodeaminase, 58K, is a peripherically associated Golgi protein, binding is tight but not dependent on presence of intact microtubules, association is likely to be mediated by a protein, dynamic component of the Golgi, a proportion of FTCD molecules cycles between the Golgi and earlier compartments of the secretory pathway
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). FTCD_RAT
541
0
58914
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
480000
-
approximately, native octameric bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4
58000
58000
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2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate
58000
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4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
58000
-
8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate
octamer
-
8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
tetramer
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4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
arrangement of subunits like a square doughnut, coupling of three subunits governs the octamer-dependent sequential enzyme activities
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding formiminotransferase cyclodeaminase is cloned and sequenced
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cDNA encoding formiminotransferase cyclodeaminase is cloned, characterized and partially sequenced
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
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bifunctional formiminotransferase cyclodeaminase provides a novel marker to study ER-Golgi dynamics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gao, Y.S.; Alvarez, C.; Nelson, D.S.; Sztul, E.
Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein
J. Biol. Chem.
273
33825-33834
1998
Rattus norvegicus
Miller, A.; Waelsch, H.
Formimino transfer from formamidinoglutaric acid to tetrahydrofolic acid
J. Biol. Chem.
228
397-417
1957
Bos taurus, Rattus norvegicus
Bashour, A.M.; Bloom, G.S.
58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase
J. Biol. Chem.
273
19612-19617
1998
Rattus norvegicus
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