EzCatDB: T00226
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DB codeT00226
CATH domainDomain 13.30.990.10 : Formiminotransferase-cyclodeaminase; Chain B, domain 1Catalytic domain
Domain 23.30.70.670 : Alpha-Beta Plaits
Domain 3-.-.-.-
E.C.2.1.2.5,4.3.1.4
CSA1qd1


Enzyme Name
UniProtKBKEGG

P53603
Protein nameFormimidoyltransferase-cyclodeaminaseglutamate 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)

SynonymsFormiminotransferase-cyclodeaminase
FTCD
IncludesGlutamate formimidoyltransferase
   EC 2.1.2.5
Glutamate formiminotransferase Glutamate formyltransferase
Formimidoyltetrahydrofolate cyclodeaminase
   EC 4.3.1.4
Formiminotetrahydrofolate cyclodeaminase
RefSeqNP_999440.1 (Protein)
NM_214275.1 (DNA/RNA sequence)
PfamPF02971 (FTCD)
PF04961 (FTCD_C)
PF07837 (FTCD_N)
[Graphical view]

KEGG pathways
MAP codePathwaysE.C.
MAP00340Histidine metabolism2.1.2.5
MAP00670One carbon pool by folate2.1.2.5,4.3.1.4

UniProtKB:Accession NumberP53603
Entry nameFTCD_PIG
Activity5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.,5-formyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formyl-L-glutamate.,5-formimidoyltetrahydrofolate = 5,10- methenyltetrahydrofolate + NH(3).
SubunitHomooctamer, including four polyglutamate binding sites. The subunits are arranged as a tetramer of dimers, and form a planar ring-shaped structure.
Subcellular locationCytoplasm (By similarity). Golgi apparatus (By similarity).
CofactorPyridoxal phosphate.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00018C00101C00439C01045C00664C00664C03479C00025C00445C00014
E.C.
2.1.2.52.1.2.52.1.2.54.3.1.42.1.2.52.1.2.52.1.2.54.3.1.44.3.1.4
CompoundPyridoxal phosphateTetrahydrofolateN-Formimino-L-glutamateN-Formyl-L-glutamate5-Formiminotetrahydrofolate5-Formiminotetrahydrofolate5-FormyltetrahydrofolateL-Glutamate5,10-MethenyltetrahydrofolateNH3
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamino acids,carboxyl group,imine groupamino acids,amide group,carboxyl groupamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,carboxyl groupamino acids,carboxyl groupamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamine group,organic ion
ChEBI18405
15635
20506
7274
48309
15639
15639
63606
16015

16134
PubChem1051
91443
5460413
439233
439376
5459780
530
5459780
530
149436
143
88747398
44272391
33032
439237
222
                  
1qd1A01UnboundUnboundUnboundUnboundUnboundAnalogue:FONUnboundUnboundUnboundUnbound
1qd1B01UnboundUnboundUnboundUnboundUnboundAnalogue:FONUnboundUnboundUnboundUnbound
1qd1A02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1qd1B02UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P53603 & literature [2]
pdbCatalytic residues
         
1qd1A01HIS   82
1qd1B01HIS 2082
1qd1A02 
1qd1B02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.7, p.43-442

references
[1]
PubMed ID10329787
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages1206-8
AuthorsKohls D, Croteau N, Mejia N, MacKenzie RE, Vrielink A
TitleCrystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-326
Medline ID20139690
PubMed ID10673422
JournalStructure Fold Des
Year2000
Volume8
Pages35-46
AuthorsKohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A
TitleThe crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.
Related PDB1qd1
Related UniProtKBP53603

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.

createdupdated
2004-03-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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