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Protein

Formimidoyltransferase-cyclodeaminase

Gene

Ftcd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool (By similarity).By similarity
Binds and promotes bundling of vimentin filaments originating from the Golgi.By similarity

Catalytic activityi

5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.
5-formyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formyl-L-glutamate.
5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3.

Cofactori

Pathwayi: L-histidine degradation into L-glutamate

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from N-formimidoyl-L-glutamate (transferase route).
Proteins known to be involved in this subpathway in this organism are:
  1. Formimidoyltransferase-cyclodeaminase (Ftcd)
This subpathway is part of the pathway L-histidine degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from N-formimidoyl-L-glutamate (transferase route), the pathway L-histidine degradation into L-glutamate and in Amino-acid degradation.

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821For formimidoyltransferase activityBy similarity
Active sitei412 – 4121For cyclodeaminase activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Biological processi

Histidine metabolism

Keywords - Ligandi

Folate-binding, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MMU-70921. Histidine catabolism.
UniPathwayiUPA00193.
UPA00379; UER00555.

Names & Taxonomyi

Protein namesi
Recommended name:
Formimidoyltransferase-cyclodeaminase
Alternative name(s):
Formiminotransferase-cyclodeaminase
Short name:
FTCD
Including the following 2 domains:
Glutamate formimidoyltransferase (EC:2.1.2.5)
Alternative name(s):
Glutamate formiminotransferase
Glutamate formyltransferase
Formimidoyltetrahydrofolate cyclodeaminase (EC:4.3.1.4)
Alternative name(s):
Formiminotetrahydrofolate cyclodeaminase
Gene namesi
Name:Ftcd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1339962. Ftcd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Formimidoyltransferase-cyclodeaminasePRO_0000087360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei520 – 5201PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91XD4.
MaxQBiQ91XD4.
PaxDbiQ91XD4.
PRIDEiQ91XD4.

PTM databases

iPTMnetiQ91XD4.
PhosphoSiteiQ91XD4.
SwissPalmiQ91XD4.

Expressioni

Gene expression databases

BgeeiQ91XD4.
CleanExiMM_FTCD.
GenevisibleiQ91XD4. MM.

Interactioni

Subunit structurei

Homooctamer, including four polyglutamate binding sites. The subunits are arranged as a tetramer of dimers, and form a planar ring-shaped structure (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199754. 1 interaction.
IntActiQ91XD4. 2 interactions.
MINTiMINT-1869900.
STRINGi10090.ENSMUSP00000001183.

Structurei

3D structure databases

ProteinModelPortaliQ91XD4.
SMRiQ91XD4. Positions 2-541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 181181Formiminotransferase N-subdomainBy similarityAdd
BLAST
Regioni163 – 17210Folate bindingSequence analysis
Regioni182 – 326145Formiminotransferase C-subdomainBy similarityAdd
BLAST
Regioni327 – 3348LinkerBy similarity
Regioni335 – 541207Cyclodeaminase/cyclohydrolaseBy similarityAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the cyclodeaminase/cyclohydrolase family.Curated
In the N-terminal section; belongs to the formiminotransferase family.Curated

Phylogenomic databases

eggNOGiENOG410IERX. Eukaryota.
COG3404. LUCA.
COG3643. LUCA.
GeneTreeiENSGT00390000005581.
HOGENOMiHOG000006949.
HOVERGENiHBG000168.
InParanoidiQ91XD4.
KOiK13990.
OMAiCEKENLF.
OrthoDBiEOG7N63MS.
PhylomeDBiQ91XD4.
TreeFamiTF333892.

Family and domain databases

Gene3Di3.30.70.670. 1 hit.
3.30.990.10. 1 hit.
InterProiIPR007044. Cyclodeamin/CycHdrlase.
IPR013802. Formiminotransferase_C.
IPR004227. Formiminotransferase_cat.
IPR012886. Formiminotransferase_N.
IPR022384. FormiminoTrfase_subdom.
[Graphical view]
PfamiPF02971. FTCD. 1 hit.
PF04961. FTCD_C. 1 hit.
PF07837. FTCD_N. 1 hit.
[Graphical view]
SMARTiSM01221. FTCD. 1 hit.
SM01222. FTCD_N. 1 hit.
[Graphical view]
SUPFAMiSSF101262. SSF101262. 1 hit.
SSF55116. SSF55116. 2 hits.
TIGRFAMsiTIGR02024. FtcD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91XD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLVECVPN FSEGNNQEVI DAISRAISQT PGCVLLDVDA GPSTNRTVYT
60 70 80 90 100
FVGQPECVVE GALHAARTAS QLIDMSKHKG EHPRMGALDV CPFIPVRGVS
110 120 130 140 150
MEECVLCAKA FGQRLAEELN VPVYLYGEAA QTPSRQTLPA IRAGEYEALP
160 170 180 190 200
EKLKQAEWVP DFGPSSFVPS WGATVTGARK FLIAFNINLL STKEQAHRIA
210 220 230 240 250
LNLREQGRGK DQPGRLKKVQ GIGWYLEEKN LAQVSTNLLD FEVTALHTVF
260 270 280 290 300
EEARREAQEL NLPVVGSQLV GLVPLKALLD AAAFYCDKEK LFVLEEEHRI
310 320 330 340 350
RLVVNRLGLD SLAPFDPKER IIEYLVPDSG PEQSLLDTSL RGFVREVGAR
360 370 380 390 400
SAAPGGGSVA AAVAALGAAL ASMVGQMTYG RRQFDHLDST MRRLIPPFHA
410 420 430 440 450
ASAQLTSLVD ADARAFAACL EAIKLPKNTP EERDRRACAL QEGLRQAVAV
460 470 480 490 500
PLKLAETVSQ LWPALQELAH CGNLSCLSDL QVAAKALETG VFGAYFNVLI
510 520 530 540
NLKDMTDDVF KEKTHHRISS LLQEAKTQAA LVLGSLEARK E
Length:541
Mass (Da):58,939
Last modified:December 1, 2001 - v1
Checksum:i988DDAC3847F5BC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC010813 mRNA. Translation: AAH10813.1.
BC024078 mRNA. Translation: AAH24078.1.
CCDSiCCDS23950.1.
RefSeqiNP_543121.1. NM_080845.2.
UniGeneiMm.36278.

Genome annotation databases

EnsembliENSMUST00000001183; ENSMUSP00000001183; ENSMUSG00000001155.
GeneIDi14317.
KEGGimmu:14317.
UCSCiuc007fut.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC010813 mRNA. Translation: AAH10813.1.
BC024078 mRNA. Translation: AAH24078.1.
CCDSiCCDS23950.1.
RefSeqiNP_543121.1. NM_080845.2.
UniGeneiMm.36278.

3D structure databases

ProteinModelPortaliQ91XD4.
SMRiQ91XD4. Positions 2-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199754. 1 interaction.
IntActiQ91XD4. 2 interactions.
MINTiMINT-1869900.
STRINGi10090.ENSMUSP00000001183.

PTM databases

iPTMnetiQ91XD4.
PhosphoSiteiQ91XD4.
SwissPalmiQ91XD4.

Proteomic databases

EPDiQ91XD4.
MaxQBiQ91XD4.
PaxDbiQ91XD4.
PRIDEiQ91XD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001183; ENSMUSP00000001183; ENSMUSG00000001155.
GeneIDi14317.
KEGGimmu:14317.
UCSCiuc007fut.2. mouse.

Organism-specific databases

CTDi10841.
MGIiMGI:1339962. Ftcd.

Phylogenomic databases

eggNOGiENOG410IERX. Eukaryota.
COG3404. LUCA.
COG3643. LUCA.
GeneTreeiENSGT00390000005581.
HOGENOMiHOG000006949.
HOVERGENiHBG000168.
InParanoidiQ91XD4.
KOiK13990.
OMAiCEKENLF.
OrthoDBiEOG7N63MS.
PhylomeDBiQ91XD4.
TreeFamiTF333892.

Enzyme and pathway databases

UniPathwayiUPA00193.
UPA00379; UER00555.
ReactomeiR-MMU-70921. Histidine catabolism.

Miscellaneous databases

NextBioi285755.
PROiQ91XD4.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XD4.
CleanExiMM_FTCD.
GenevisibleiQ91XD4. MM.

Family and domain databases

Gene3Di3.30.70.670. 1 hit.
3.30.990.10. 1 hit.
InterProiIPR007044. Cyclodeamin/CycHdrlase.
IPR013802. Formiminotransferase_C.
IPR004227. Formiminotransferase_cat.
IPR012886. Formiminotransferase_N.
IPR022384. FormiminoTrfase_subdom.
[Graphical view]
PfamiPF02971. FTCD. 1 hit.
PF04961. FTCD_C. 1 hit.
PF07837. FTCD_N. 1 hit.
[Graphical view]
SMARTiSM01221. FTCD. 1 hit.
SM01222. FTCD_N. 1 hit.
[Graphical view]
SUPFAMiSSF101262. SSF101262. 1 hit.
SSF55116. SSF55116. 2 hits.
TIGRFAMsiTIGR02024. FtcD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiFTCD_MOUSE
AccessioniPrimary (citable) accession number: Q91XD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.