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P53603

- FTCD_PIG

UniProt

P53603 - FTCD_PIG

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Protein

Formimidoyltransferase-cyclodeaminase

Gene

FTCD

Organism
Sus scrofa (Pig)
Status
Reviewed - 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

Sites

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

GO - Molecular functioni

  1. folic acid binding Source: UniProtKB-KW
  2. formimidoyltetrahydrofolate cyclodeaminase activity Source: UniProtKB-EC
  3. glutamate formimidoyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
  2. histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway
  3. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Biological processi

Histidine metabolism

Keywords - Ligandi

Folate-binding, Pyridoxal phosphate

Enzyme and pathway databases

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
ProteomesiUP000008227: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Formimidoyltransferase-cyclodeaminasePRO_0000087361Add
BLAST

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.

Structurei

Secondary structure

1
541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 123Combined sources
Helixi17 – 2812Combined sources
Beta strandi34 – 418Combined sources
Turni42 – 454Combined sources
Beta strandi46 – 538Combined sources
Helixi55 – 7218Combined sources
Helixi75 – 773Combined sources
Beta strandi85 – 9814Combined sources
Helixi101 – 11919Combined sources
Beta strandi123 – 1275Combined sources
Helixi133 – 1353Combined sources
Helixi138 – 1425Combined sources
Helixi145 – 1528Combined sources
Helixi156 – 1583Combined sources
Beta strandi161 – 1633Combined sources
Turni169 – 1713Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi183 – 1919Combined sources
Helixi193 – 20311Combined sources
Beta strandi219 – 2268Combined sources
Turni227 – 2304Combined sources
Beta strandi231 – 2399Combined sources
Turni241 – 2433Combined sources
Helixi246 – 25914Combined sources
Beta strandi264 – 2718Combined sources
Helixi275 – 28915Combined sources
Helixi296 – 30712Combined sources
Turni308 – 3103Combined sources
Beta strandi311 – 3133Combined sources
Helixi317 – 3204Combined sources
Helixi322 – 3254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QD1X-ray1.70A/B2-326[»]
ProteinModelPortaliP53603.
SMRiP53603. Positions 2-540.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53603.

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

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_N/C_subdom.
[Graphical view]
PfamiPF02971. FTCD. 1 hit.
PF04961. FTCD_C. 1 hit.
PF07837. 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 .
PIRi A48717.
RefSeqi NP_999440.1. NM_214275.1.
UniGenei Ssc.16313.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QD1 X-ray 1.70 A/B 2-326 [» ]
ProteinModelPortali P53603.
SMRi P53603. Positions 2-540.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397517.
KEGGi ssc:397517.

Organism-specific databases

CTDi 10841.

Phylogenomic databases

HOVERGENi HBG000168.
InParanoidi P53603.
KOi K13990.

Enzyme and pathway databases

UniPathwayi UPA00193 .
UPA00379 ; UER00555 .
SABIO-RK P53603.

Miscellaneous databases

EvolutionaryTracei P53603.

Family and domain databases

Gene3Di 3.30.70.670. 1 hit.
3.30.990.10. 1 hit.
InterProi IPR007044. Cyclodeamin/CycHdrlase.
IPR013802. Formiminotransferase_C.
IPR004227. Formiminotransferase_cat.
IPR012886. Formiminotransferase_N.
IPR022384. FormiminoTrfase_N/C_subdom.
[Graphical view ]
Pfami PF02971. FTCD. 1 hit.
PF04961. FTCD_C. 1 hit.
PF07837. FTCD_N. 1 hit.
[Graphical view ]
SUPFAMi SSF101262. SSF101262. 1 hit.
SSF55116. SSF55116. 2 hits.
TIGRFAMsi TIGR02024. FtcD. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

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 26, 2014
This is version 101 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

External Data

Dasty 3