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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821For formimidoyltransferase activityBy similarity
Active sitei412 – 4121For cyclodeaminase activity1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Formimidoyltransferase-cyclodeaminasePRO_0000087362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei520 – 5201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO88618.
PRIDEiO88618.

PTM databases

iPTMnetiO88618.
PhosphoSiteiO88618.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

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

1
541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Helixi17 – 2610Combined sources
Turni27 – 293Combined sources
Beta strandi33 – 419Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 538Combined sources
Helixi55 – 7016Combined sources
Helixi75 – 773Combined sources
Beta strandi86 – 883Combined sources
Beta strandi90 – 989Combined sources
Helixi101 – 11919Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi135 – 1373Combined sources
Helixi138 – 1414Combined sources
Helixi149 – 1524Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi183 – 1919Combined sources
Helixi193 – 20311Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi219 – 2268Combined sources
Turni227 – 2304Combined sources
Beta strandi231 – 2399Combined sources
Turni241 – 2433Combined sources
Helixi246 – 25813Combined sources
Turni259 – 2613Combined sources
Beta strandi264 – 2718Combined sources
Helixi275 – 28915Combined sources
Helixi296 – 30510Combined sources
Beta strandi310 – 3134Combined sources
Helixi317 – 3204Combined sources
Helixi322 – 3254Combined sources
Helixi335 – 3373Combined sources
Helixi340 – 3478Combined sources
Beta strandi352 – 3543Combined sources
Helixi357 – 37721Combined sources
Beta strandi379 – 3813Combined sources
Helixi385 – 3873Combined sources
Helixi388 – 40619Combined sources
Helixi408 – 42316Combined sources
Helixi430 – 4323Combined sources
Turni433 – 4353Combined sources
Helixi436 – 46833Combined sources
Helixi477 – 50226Combined sources
Helixi508 – 53932Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO88618.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 181181Formiminotransferase N-subdomainAdd
BLAST
Regioni163 – 17210Folate bindingSequence analysis
Regioni182 – 326145Formiminotransferase C-subdomainAdd
BLAST
Regioni327 – 3348Linker
Regioni335 – 541207Cyclodeaminase/cyclohydrolaseAdd
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.
InParanoidiO88618.
KOiK13990.
OMAiCEKENLF.
OrthoDBiEOG7N63MS.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1TT9X-ray3.42A/B/C/D1-541[»]
2PFDX-ray3.42A/B/C/D1-541[»]
ProteinModelPortaliO88618.
SMRiO88618. Positions 2-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4577997.
STRINGi10116.ENSRNOP00000001699.

PTM databases

iPTMnetiO88618.
PhosphoSiteiO88618.

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.
OrthoDBiEOG7N63MS.
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

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...

Publicationsi

« Hide 'large scale' publications
  1. Gao Y.-S., Sztul E.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 257.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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.
  3. "Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein."
    Gao Y.-S., Alvarez C., Nelson D.S., Sztul E.
    J. Biol. Chem. 273:33825-33834(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-48; 88-179 AND 223-285.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase."
    Bashour A.-M., Bloom G.S.
    J. Biol. Chem. 273:19612-19617(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 48-65; 115-136; 156-165; 257-268; 291-299; 307-318; 321-341 AND 394-413, SUBCELLULAR LOCATION.
    Tissue: Liver.
  5. "A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein."
    Gao Y.S., Vrielink A., MacKenzie R., Sztul E.
    Eur. J. Cell Biol. 81:391-401(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer."
    Mao Y., Vyas N.K., Vyas M.N., Chen D.H., Ludtke S.J., Chiu W., Quiocho F.A.
    EMBO J. 23:2963-2971(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS), SUBUNIT, ACTIVE SITE FOR CYCLODEAMINASE ACTIVITY.
  8. "Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-A crystallographic resolution."
    Poon B.K., Chen X., Lu M., Vyas N.K., Quiocho F.A., Wang Q., Ma J.
    Proc. Natl. Acad. Sci. U.S.A. 104:7869-7874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS), SUBUNIT.

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: June 8, 2016
This is version 143 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.