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Protein

Formimidoyltransferase-cyclodeaminase

Gene

Ftcd

Organism
Rattus norvegicus (Rat)
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.1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei82For formimidoyltransferase activityBy similarity1
Active sitei412For cyclodeaminase activity1 Publication1

GO - Molecular functioni

  • folic acid binding Source: UniProtKB-KW
  • formimidoyltetrahydrofolate cyclodeaminase activity Source: BHF-UCL
  • formimidoyltransferase activity Source: BHF-UCL
  • glutamate formimidoyltransferase activity Source: RGD
  • intermediate filament binding Source: RGD
  • microtubule binding Source: BHF-UCL

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

BRENDAi2.1.2.5. 5301.
4.3.1.4. 5301.
ReactomeiR-RNO-70921. Histidine catabolism.
UniPathwayiUPA00193.
UPA00379; UER00555.

Names & Taxonomyi

Protein namesi
Recommended name:
Formimidoyltransferase-cyclodeaminase
Alternative name(s):
58 kDa microtubule-binding protein
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi70915. Ftcd.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB-SubCell
  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: BHF-UCL
  • endoplasmic reticulum-Golgi intermediate compartment Source: BHF-UCL
  • extracellular exosome Source: Ensembl
  • Golgi apparatus Source: RGD
  • Golgi membrane Source: BHF-UCL
  • smooth endoplasmic reticulum membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000873621 – 541Formimidoyltransferase-cyclodeaminaseAdd BLAST541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei520PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO88618.
PRIDEiO88618.

PTM databases

iPTMnetiO88618.
PhosphoSitePlusiO88618.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSRNOG00000001261.
GenevisibleiO88618. RN.

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.2 Publications

GO - Molecular functioni

  • intermediate filament binding Source: RGD
  • microtubule binding Source: BHF-UCL

Protein-protein interaction databases

MINTiMINT-4577997.
STRINGi10116.ENSRNOP00000001699.

Structurei

Secondary structure

1541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Helixi17 – 26Combined sources10
Turni27 – 29Combined sources3
Beta strandi33 – 41Combined sources9
Turni42 – 45Combined sources4
Beta strandi46 – 53Combined sources8
Helixi55 – 70Combined sources16
Helixi75 – 77Combined sources3
Beta strandi86 – 88Combined sources3
Beta strandi90 – 98Combined sources9
Helixi101 – 119Combined sources19
Beta strandi123 – 127Combined sources5
Beta strandi135 – 137Combined sources3
Helixi138 – 141Combined sources4
Helixi149 – 152Combined sources4
Beta strandi156 – 158Combined sources3
Beta strandi161 – 163Combined sources3
Beta strandi174 – 178Combined sources5
Beta strandi183 – 191Combined sources9
Helixi193 – 203Combined sources11
Beta strandi208 – 212Combined sources5
Beta strandi219 – 226Combined sources8
Turni227 – 230Combined sources4
Beta strandi231 – 239Combined sources9
Turni241 – 243Combined sources3
Helixi246 – 258Combined sources13
Turni259 – 261Combined sources3
Beta strandi264 – 271Combined sources8
Helixi275 – 289Combined sources15
Helixi296 – 305Combined sources10
Beta strandi310 – 313Combined sources4
Helixi317 – 320Combined sources4
Helixi322 – 325Combined sources4
Helixi335 – 337Combined sources3
Helixi340 – 347Combined sources8
Beta strandi352 – 354Combined sources3
Helixi357 – 377Combined sources21
Beta strandi379 – 381Combined sources3
Helixi385 – 387Combined sources3
Helixi388 – 406Combined sources19
Helixi408 – 423Combined sources16
Helixi430 – 432Combined sources3
Turni433 – 435Combined sources3
Helixi436 – 468Combined sources33
Helixi477 – 502Combined sources26
Helixi508 – 539Combined sources32

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TT9X-ray3.42A/B/C/D1-541[»]
2PFDX-ray3.42A/B/C/D1-541[»]
ProteinModelPortaliO88618.
SMRiO88618.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88618.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 181Formiminotransferase N-subdomainAdd BLAST181
Regioni163 – 172Folate bindingSequence analysis10
Regioni182 – 326Formiminotransferase C-subdomainAdd BLAST145
Regioni327 – 334Linker8
Regioni335 – 541Cyclodeaminase/cyclohydrolaseAdd BLAST207

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.
InParanoidiO88618.
KOiK13990.
OMAiCEKENLF.
OrthoDBiEOG091G0950.
PhylomeDBiO88618.
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.

O88618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLVECVPN FSEGNNQEVI DAISQAISQT PGCVLLDVDA GPSTNRTVYT
60 70 80 90 100
FVGQPECVVE GALSAARTAS QLIDMRKHKG EHPRMGALDV CPFIPVRGVS
110 120 130 140 150
MDECVLCAKA FGQRLAEELN VPVYLYGEAA QMPSRQTLPA IRAGEYEALP
160 170 180 190 200
EKLKQAEWVP DFGPSSFVPS WGATVTGARK FLIAFNINLL STKEQAHRIA
210 220 230 240 250
LNLREQGRGK DQPGRLKKVQ GIGWYLEEKN LAQVSTNLLD FEVTALHTVY
260 270 280 290 300
EEARREAQEL NLPVVGSQLV GLVPLKALLD AAAFYCDKEK LFVLEEEHRI
310 320 330 340 350
RLVVNRLGLD SLAPFDPKER IIEYLVPDSG PEQSLLDASL RAFVREVGAR
360 370 380 390 400
SAAPGGGSVA AAVAALGAAL ASMVGQMTYG RRQFDHLDST MRRLIPPFHA
410 420 430 440 450
ASAQLTSLVD ADARAFAACL GAIKLPKNTP EERDRRTCAL QEGLRQAVAV
460 470 480 490 500
PLKLAETVSQ LWPALQELAQ CGNLSCLSDL QVAAKALETG VFGAYFNVLI
510 520 530 540
NLKDMTDDVF KEKTRHRISS LLQEAKTQAA LVLGSLEARK E
Length:541
Mass (Da):58,914
Last modified:June 6, 2002 - v4
Checksum:i76D806CE23478D92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079233 mRNA. Translation: AAC28849.3.
BC091134 mRNA. Translation: AAH91134.1.
RefSeqiNP_446019.1. NM_053567.1.
UniGeneiRn.20140.

Genome annotation databases

EnsembliENSRNOT00000001699; ENSRNOP00000001699; ENSRNOG00000001261.
GeneIDi89833.
KEGGirno:89833.
UCSCiRGD:70915. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079233 mRNA. Translation: AAC28849.3.
BC091134 mRNA. Translation: AAH91134.1.
RefSeqiNP_446019.1. NM_053567.1.
UniGeneiRn.20140.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TT9X-ray3.42A/B/C/D1-541[»]
2PFDX-ray3.42A/B/C/D1-541[»]
ProteinModelPortaliO88618.
SMRiO88618.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4577997.
STRINGi10116.ENSRNOP00000001699.

PTM databases

iPTMnetiO88618.
PhosphoSitePlusiO88618.

Proteomic databases

PaxDbiO88618.
PRIDEiO88618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001699; ENSRNOP00000001699; ENSRNOG00000001261.
GeneIDi89833.
KEGGirno:89833.
UCSCiRGD:70915. rat.

Organism-specific databases

CTDi10841.
RGDi70915. Ftcd.

Phylogenomic databases

eggNOGiENOG410IERX. Eukaryota.
COG3404. LUCA.
COG3643. LUCA.
GeneTreeiENSGT00390000005581.
HOGENOMiHOG000006949.
HOVERGENiHBG000168.
InParanoidiO88618.
KOiK13990.
OMAiCEKENLF.
OrthoDBiEOG091G0950.
PhylomeDBiO88618.
TreeFamiTF333892.

Enzyme and pathway databases

UniPathwayiUPA00193.
UPA00379; UER00555.
BRENDAi2.1.2.5. 5301.
4.3.1.4. 5301.
ReactomeiR-RNO-70921. Histidine catabolism.

Miscellaneous databases

EvolutionaryTraceiO88618.
PROiO88618.

Gene expression databases

BgeeiENSRNOG00000001261.
GenevisibleiO88618. RN.

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...

Entry informationi

Entry nameiFTCD_RAT
AccessioniPrimary (citable) accession number: O88618
Secondary accession number(s): Q5BKB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 6, 2002
Last modified: November 2, 2016
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.