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Information on EC 4.3.1.4 - formimidoyltetrahydrofolate cyclodeaminase and Organism(s) Rattus norvegicus and UniProt Accession O88618

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.4 formimidoyltetrahydrofolate cyclodeaminase
IUBMB Comments
In eukaroytes, occurs as a bifunctional enzyme that also has glutamate formimidoyltransferase (EC 2.1.2.5) activity.
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This record set is specific for:
Rattus norvegicus
UNIPROT: O88618
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
formiminotransferase cyclodeaminase, 58k golgi protein, formiminotetrahydrofolate cyclodeaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deaminase, formiminotetrahydrofolate cyclo-
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-
-
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formimino-THF cyclodeaminase
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-
-
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Formiminotetrahydrofolate cyclodeaminase
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-
-
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formiminotransferase cyclodeaminase
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-
-
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FTCD
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing; 5,10-methenyltetrahydrofolate-forming)
In eukaroytes, occurs as a bifunctional enzyme that also has glutamate formimidoyltransferase (EC 2.1.2.5) activity.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-05-7
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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
5-formiminotetrahydrofolate
5,10-methenyltetrahydrofolate + NH3
show the reaction diagram
5-formiminotetrahydrofolate
?
show the reaction diagram
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-
-
-
?
additional information
?
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-
folate-dependent bifunctional enzyme formiminoglutamate: tetrahydrofolate formiminotransferase-formiminotetrahydrofolate cyclodeaminase catalyzes two sequential reactions of the histidine degradation pathway
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-
?
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-formiminotetrahydrofolate
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
folate-dependent bifunctional enzyme formiminoglutamate: tetrahydrofolate formiminotransferase-formiminotetrahydrofolate cyclodeaminase catalyzes two sequential reactions of the histidine degradation pathway
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
activates
NH4+
-
activates
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
Golgi apparatus, formiminotransferase-cyclodeaminase enzyme complex
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FTCD_RAT
541
0
58914
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to space group P4 with unit cell dimensions of a = b = 134.85 A and c = 156.37 A and four subunits in the asymmetric unit for a total of 32 selenium atoms
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
formiminotransferase-cyclodeaminase enzyme complex
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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formiminotransferase cyclodeaminase enzyme complex represents a marker with which to explore ER-Golgi dynamics
medicine
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23 out of 38 patients with type 2 autoimmune hepatitis are positive for antibodies against enzyme, epitopes are mainly in formiminotransferase region
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooperman, J.M.
Formimino-L-glutamate
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
8
514-521
1985
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Hennig, D.; Scales, S.J.; Moreau, A.; Murley, L.L.; De Mey, J.; Kreis, T.E.
A formiminotransferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules
J. Biol. Chem.
273
19602-19611
1998
Canis lupus familiaris, Canis lupus familiaris Madin-Darby, Gallus gallus (Q9YH58), Gallus gallus, Homo sapiens, Meleagris gallopavo, Rattus norvegicus, Sus scrofa (P53603)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Muratori, L.; Sztul, E.; Muratori, P.; Gao, Y.; Ripalti, A.; Ponti, C.; Lenzi, M.; Landini, M.P.; Bianchi, F.B.
Distinct epitopes on formiminotransferase cyclodeaminase induce autoimmune liver cytosol antibody type 1
Hepatology
34
494-501
2001
Rattus norvegicus
Manually annotated by BRENDA team
Mao, Y.; Vyas, N.K.; Vyas, M.N.; Chen, D.H.; Ludtke, S.J.; Chiu, W.; Quiocho, F.A.
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer
EMBO J.
23
2963-2971
2004
Rattus norvegicus (O88618)
Manually annotated by BRENDA team