DB code: T00226

CATH domain 3.30.990.10 : Formiminotransferase-cyclodeaminase; Chain B, domain 1 Catalytic domain
3.30.70.670 : Alpha-Beta Plaits
-.-.-.- :
E.C. 2.1.2.5 4.3.1.4
CSA 1qd1
M-CSA 1qd1
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Includes RefSeq Pfam
P53603 Formimidoyltransferase-cyclodeaminase
Formiminotransferase-cyclodeaminase
FTCD
Glutamate formimidoyltransferase
EC 2.1.2.5
Glutamate formiminotransferase Glutamate formyltransferase
Formimidoyltetrahydrofolate cyclodeaminase
EC 4.3.1.4
Formiminotetrahydrofolate cyclodeaminase
NP_999440.1 (Protein)
NM_214275.1 (DNA/RNA sequence)
PF02971 (FTCD)
PF04961 (FTCD_C)
PF07837 (FTCD_N)
[Graphical View]

KEGG enzyme name
glutamate formimidoyltransferase
(EC 2.1.2.5 )
glutamate formyltransferase
(EC 2.1.2.5 )
formiminoglutamic acid transferase
(EC 2.1.2.5 )
formiminoglutamic formiminotransferase
(EC 2.1.2.5 )
glutamate formiminotransferase
(EC 2.1.2.5 )
formimidoyltetrahydrofolate cyclodeaminase
(EC 4.3.1.4 )
formiminotetrahydrofolate cyclodeaminase
(EC 4.3.1.4 )
5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing)
(EC 4.3.1.4 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P53603 FTCD_PIG 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate. 5-formyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formyl-L-glutamate. 5-formimidoyltetrahydrofolate = 5,10- methenyltetrahydrofolate + NH(3). Homooctamer, including four polyglutamate binding sites. The subunits are arranged as a tetramer of dimers, and form a planar ring-shaped structure. Cytoplasm (By similarity). Golgi apparatus (By similarity). Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00340 Histidine metabolism 2.1.2.5
MAP00670 One carbon pool by folate 2.1.2.5 4.3.1.4

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C00101 C00439 C01045 C00664 C00664 C03479 C00025 C00445 C00014
E.C. 2.1.2.5
2.1.2.5
2.1.2.5
4.3.1.4
2.1.2.5
2.1.2.5
2.1.2.5
4.3.1.4
4.3.1.4
Compound Pyridoxal phosphate Tetrahydrofolate N-Formimino-L-glutamate N-Formyl-L-glutamate 5-Formiminotetrahydrofolate 5-Formiminotetrahydrofolate 5-Formyltetrahydrofolate L-Glutamate 5,10-Methenyltetrahydrofolate NH3
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group amino acids,carboxyl group,imine group amino acids,amide group,carboxyl group amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,carboxyl group amino acids,carboxyl group amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group amine group,organic ion
ChEBI 18405
 18405
 		15635
 20506
 15635
 20506
 		7274
 7274
 		48309
 48309
 		15639
 15639
 		15639
 15639
 		63606
 63606
 		16015
 16015
 		16134
 16134
PubChem 1051
 1051
 		5460413
 91443
 5460413
 91443
 		439233
 439233
 		439376
 439376
 		530
 5459780
 530
 5459780
 		530
 5459780
 530
 5459780
 		143
 149436
 143
 149436
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
 		439237
 439237
 		222
 222
1qd1A01 Unbound Unbound Unbound Unbound Unbound Analogue:FON Unbound Unbound Unbound Unbound
1qd1B01 Unbound Unbound Unbound Unbound Unbound Analogue:FON Unbound Unbound Unbound Unbound
1qd1A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qd1B02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P53603 & literature [2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1qd1A01 HIS 82
1qd1B01 HIS 2082
1qd1A02
1qd1B02

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.7, p.43-44 2

References
[1]
Resource
Comments
Medline ID
PubMed ID 10329787
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 1206-8
Authors Kohls D, Croteau N, Mejia N, MacKenzie RE, Vrielink A
Title Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-326
Medline ID 20139690
PubMed ID 10673422
Journal Structure Fold Des
Year 2000
Volume 8
Pages 35-46
Authors Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A
Title The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.
Related PDB 1qd1
Related UniProtKB P53603

Comments
This enzyme is a bifunctional enzyme with glutamate formiminotransferase (EC 2.1.2.5) and formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4). PDB structure, 1qd1, corresponds to the N-terminal domain of glutamate formiminotransferase (EC 2.1.2.5). The structure of the remainder has not been reported.

Created Updated
2004-03-17 2009-02-26