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P53603 (FTCD_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formimidoyltransferase-cyclodeaminase
Alternative name(s):
Formiminotransferase-cyclodeaminase
Short name=FTCD

Including the following 2 domains:

  1. Glutamate formimidoyltransferase
    EC=2.1.2.5
    Alternative name(s):
    Glutamate formiminotransferase
    Glutamate formyltransferase
  2. Formimidoyltetrahydrofolate cyclodeaminase
    EC=4.3.1.4
    Alternative name(s):
    Formiminotetrahydrofolate cyclodeaminase
Gene names
Name:FTCD
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate.

5-formyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formyl-L-glutamate.

5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1.

One-carbon metabolism; tetrahydrofolate interconversion.

Subunit structure

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

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Golgi apparatus By similarity. Note: More abundantly located around the mother centriole By similarity.

Sequence similarities

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

In the N-terminal section; belongs to the formiminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Formimidoyltransferase-cyclodeaminase
PRO_0000087361

Regions

Region1 – 181181Formiminotransferase N-subdomain By similarity
Region163 – 17210Folate binding Potential
Region182 – 326145Formiminotransferase C-subdomain By similarity
Region327 – 3348Linker By similarity
Region335 – 541207Cyclodeaminase/cyclohydrolase By similarity

Sites

Active site821For formimidoyltransferase activity Probable
Active site4121For cyclodeaminase activity By similarity

Secondary structure

........................................................... 541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53603 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D52974A9EE088DDF

FASTA54158,930
        10         20         30         40         50         60 
MSQLVECVPN FSEGKNQEVI DAISRAVAQT PGCVLLDVDS GPSTNRTVYT FVGRPEDVVE 

        70         80         90        100        110        120 
GALNAARAAY QLIDMSRHHG EHPRMGALDV CPFIPVRGVT MDECVRCAQA FGQRLAEELG 

       130        140        150        160        170        180 
VPVYLYGEAA RTAGRQSLPA LRAGEYEALP EKLKQAEWAP DFGPSAFVPS WGATVAGARK 

       190        200        210        220        230        240 
FLLAFNINLL STREQAHRIA LDLREQGRGK DQPGRLKKVQ AIGWYLDEKN LAQVSTNLLD 

       250        260        270        280        290        300 
FEVTGLHTVF EETCREAQEL SLPVVGSQLV GLVPLKALLD AAAFYCEKEN LFLLQDEHRI 

       310        320        330        340        350        360 
RLVVNRLGLD SLAPFKPKER IIEYLVPEAG PEQSLLHKPL RTFVREVGSR SAAPGAGSVA 

       370        380        390        400        410        420 
AATAAMGAAL ASMVGLMTYG RRQFEHLDAT MRRLIPPFHA ASAKLTSLVD ADARAFEAYL 

       430        440        450        460        470        480 
KAMKLPKDTP EDKDRRAAAL QEGLRQAVAV PLALAETVAS LWPALQELAL CGNLACRSDL 

       490        500        510        520        530        540 
QVAAKALETG VFGAYFNVLI NLKDVTDDAF KAQVRQRISS LLQEAKTQAA LVLDRLEARQ 


A 

« Hide

References

[1]"The nucleotide sequence of porcine formiminotransferase cyclodeaminase. Expression and purification from Escherichia coli."
Murley L.L., Mejia N.R., Mackenzie R.E.
J. Biol. Chem. 268:22820-22824(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 392-410 AND 424-453.
Strain: Yucatan.
Tissue: Liver.
[2]"The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme."
Kohls D., Sulea T., Purisima E.O., MacKenzie R.E., Vrielink A.
Structure 8:35-46(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-326.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16507 mRNA. Translation: AAA31034.1.
PIRA48717.
RefSeqNP_999440.1. NM_214275.1.
UniGeneSsc.16313.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QD1X-ray1.70A/B2-326[»]
ProteinModelPortalP53603.
SMRP53603. Positions 2-540.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397517.
KEGGssc:397517.

Organism-specific databases

CTD10841.

Phylogenomic databases

HOVERGENHBG000168.
KOK13990.

Enzyme and pathway databases

SABIO-RKP53603.
UniPathwayUPA00193.
UPA00379; UER00555.

Family and domain databases

Gene3D3.30.70.670. 1 hit.
3.30.990.10. 1 hit.
InterProIPR007044. Cyclodeamin/CycHdrlase.
IPR013802. Formiminotransferase_C.
IPR004227. Formiminotransferase_cat.
IPR012886. Formiminotransferase_N.
IPR022384. FormiminoTrfase_N/C_subdom.
[Graphical view]
PfamPF02971. FTCD. 1 hit.
PF04961. FTCD_C. 1 hit.
PF07837. FTCD_N. 1 hit.
[Graphical view]
SUPFAMSSF101262. SSF101262. 1 hit.
SSF55116. SSF55116. 2 hits.
TIGRFAMsTIGR02024. FtcD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP53603.

Entry information

Entry nameFTCD_PIG
AccessionPrimary (citable) accession number: P53603
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 13, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways