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Protein

Formimidoyltransferase-cyclodeaminase

Gene

FTCD

Organism
Sus scrofa (Pig)
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.
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)DescriptionActionsGraphical viewLength
Active sitei82For formimidoyltransferase activityCurated1
Active sitei412For cyclodeaminase activityBy similarity1

GO - Molecular functioni

  • folic acid binding Source: UniProtKB-KW
  • formimidoyltetrahydrofolate cyclodeaminase activity Source: BHF-UCL
  • glutamate formimidoyltransferase activity 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. 6170.
4.3.1.4. 6170.
SABIO-RKP53603.
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000873611 – 541Formimidoyltransferase-cyclodeaminaseAdd BLAST541

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei520PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP53603.
PeptideAtlasiP53603.
PRIDEiP53603.

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.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000022108.

Structurei

Secondary structure

1541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 12Combined sources3
Helixi17 – 28Combined sources12
Beta strandi34 – 41Combined sources8
Turni42 – 45Combined sources4
Beta strandi46 – 53Combined sources8
Helixi55 – 72Combined sources18
Helixi75 – 77Combined sources3
Beta strandi85 – 98Combined sources14
Helixi101 – 119Combined sources19
Beta strandi123 – 127Combined sources5
Helixi133 – 135Combined sources3
Helixi138 – 142Combined sources5
Helixi145 – 152Combined sources8
Helixi156 – 158Combined sources3
Beta strandi161 – 163Combined sources3
Turni169 – 171Combined sources3
Beta strandi174 – 178Combined sources5
Beta strandi183 – 191Combined sources9
Helixi193 – 203Combined sources11
Beta strandi219 – 226Combined sources8
Turni227 – 230Combined sources4
Beta strandi231 – 239Combined sources9
Turni241 – 243Combined sources3
Helixi246 – 259Combined sources14
Beta strandi264 – 271Combined sources8
Helixi275 – 289Combined sources15
Helixi296 – 307Combined sources12
Turni308 – 310Combined sources3
Beta strandi311 – 313Combined sources3
Helixi317 – 320Combined sources4
Helixi322 – 325Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QD1X-ray1.70A/B2-326[»]
ProteinModelPortaliP53603.
SMRiP53603.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53603.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 181Formiminotransferase N-subdomainBy similarityAdd BLAST181
Regioni163 – 172Folate bindingSequence analysis10
Regioni182 – 326Formiminotransferase C-subdomainBy similarityAdd BLAST145
Regioni327 – 334LinkerBy similarity8
Regioni335 – 541Cyclodeaminase/cyclohydrolaseBy similarityAdd 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.
HOVERGENiHBG000168.
InParanoidiP53603.
KOiK13990.

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.

P53603-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLVECVPN FSEGKNQEVI DAISRAVAQT PGCVLLDVDS GPSTNRTVYT
60 70 80 90 100
FVGRPEDVVE GALNAARAAY QLIDMSRHHG EHPRMGALDV CPFIPVRGVT
110 120 130 140 150
MDECVRCAQA FGQRLAEELG VPVYLYGEAA RTAGRQSLPA LRAGEYEALP
160 170 180 190 200
EKLKQAEWAP DFGPSAFVPS WGATVAGARK FLLAFNINLL STREQAHRIA
210 220 230 240 250
LDLREQGRGK DQPGRLKKVQ AIGWYLDEKN LAQVSTNLLD FEVTGLHTVF
260 270 280 290 300
EETCREAQEL SLPVVGSQLV GLVPLKALLD AAAFYCEKEN LFLLQDEHRI
310 320 330 340 350
RLVVNRLGLD SLAPFKPKER IIEYLVPEAG PEQSLLHKPL RTFVREVGSR
360 370 380 390 400
SAAPGAGSVA AATAAMGAAL ASMVGLMTYG RRQFEHLDAT MRRLIPPFHA
410 420 430 440 450
ASAKLTSLVD ADARAFEAYL KAMKLPKDTP EDKDRRAAAL QEGLRQAVAV
460 470 480 490 500
PLALAETVAS LWPALQELAL CGNLACRSDL QVAAKALETG VFGAYFNVLI
510 520 530 540
NLKDVTDDAF KAQVRQRISS LLQEAKTQAA LVLDRLEARQ A
Length:541
Mass (Da):58,930
Last modified:October 1, 1996 - v1
Checksum:iD52974A9EE088DDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16507 mRNA. Translation: AAA31034.1.
PIRiA48717.
RefSeqiNP_999440.1. NM_214275.1.
UniGeneiSsc.16313.

Genome annotation databases

GeneIDi397517.
KEGGissc:397517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16507 mRNA. Translation: AAA31034.1.
PIRiA48717.
RefSeqiNP_999440.1. NM_214275.1.
UniGeneiSsc.16313.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QD1X-ray1.70A/B2-326[»]
ProteinModelPortaliP53603.
SMRiP53603.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000022108.

Proteomic databases

PaxDbiP53603.
PeptideAtlasiP53603.
PRIDEiP53603.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397517.
KEGGissc:397517.

Organism-specific databases

CTDi10841.

Phylogenomic databases

eggNOGiENOG410IERX. Eukaryota.
COG3404. LUCA.
COG3643. LUCA.
HOVERGENiHBG000168.
InParanoidiP53603.
KOiK13990.

Enzyme and pathway databases

UniPathwayiUPA00193.
UPA00379; UER00555.
BRENDAi2.1.2.5. 6170.
4.3.1.4. 6170.
SABIO-RKP53603.

Miscellaneous databases

EvolutionaryTraceiP53603.

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_PIG
AccessioniPrimary (citable) accession number: P53603
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 111 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

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.