O95954 · FTCD_HUMAN
- ProteinFormimidoyltransferase-cyclodeaminase
- GeneFTCD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids541 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Catalytic activity
- 5-formimidoyltetrahydrofolate + L-glutamate = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoyl-L-glutamateThis reaction proceeds in the backward direction.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
10.2 μmol/min/mg | for the glutamate formimidoyltransferase activity |
Pathway
Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 82 | For formimidoyltransferase activity | ||||
Sequence: H | ||||||
Active site | 412 | For cyclodeaminase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centriole | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | plasma membrane | |
Cellular Component | smooth endoplasmic reticulum membrane | |
Molecular Function | folic acid binding | |
Molecular Function | formimidoyltetrahydrofolate cyclodeaminase activity | |
Molecular Function | glutamate formimidoyltransferase activity | |
Molecular Function | microtubule binding | |
Biological Process | cytoskeleton organization | |
Biological Process | folic acid-containing compound metabolic process | |
Biological Process | L-histidine catabolic process to glutamate and formamide | |
Biological Process | L-histidine catabolic process to glutamate and formate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFormimidoyltransferase-cyclodeaminase
- Alternative names
Including 2 domains:
- Recommended nameGlutamate formimidoyltransferase
- EC number
- Alternative names
- Recommended nameFormimidoyltetrahydrofolate cyclodeaminase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95954
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: More abundantly located around the mother centriole.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Glutamate formiminotransferase deficiency (FIGLU-URIA)
- Note
- DescriptionAutosomal recessive disorder. Features of a severe phenotype, include elevated levels of formiminoglutamate (FIGLU) in the urine in response to histidine administration, megaloblastic anemia, and intellectual disability. Features of a mild phenotype include high urinary excretion of FIGLU in the absence of histidine administration, mild developmental delay, and no hematological abnormalities.
- See alsoMIM:229100
Natural variants in FIGLU-URIA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_015887 | 135 | R>C | in FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 61% of wild-type activity; dbSNP:rs28941768 | |
VAR_015888 | 299 | R>P | in FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 57% wild-type activity; dbSNP:rs119469015 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_015887 | 135 | in FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 61% of wild-type activity; dbSNP:rs28941768 | |||
Sequence: R → C | ||||||
Natural variant | VAR_015888 | 299 | in FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 57% wild-type activity; dbSNP:rs119469015 | |||
Sequence: R → P | ||||||
Natural variant | VAR_015889 | 438 | ||||
Sequence: A → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 902 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000087359 | 1-541 | Formimidoyltransferase-cyclodeaminase | |||
Sequence: MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARKFLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLDFEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRIRLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVAAAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYLEAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDLQVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQE | ||||||
Modified residue | 316 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 386 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 520 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 549 | In isoform O95954-2; Phosphoserine |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homooctamer, including four polyglutamate binding sites. The subunits are arranged as a tetramer of dimers, and form a planar ring-shaped structure.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95954 | AGR2 O95994 | 3 | EBI-10192648, EBI-712648 | |
BINARY | O95954 | CCDC183 G5E9W6 | 3 | EBI-10192648, EBI-17212717 | |
BINARY | O95954 | HGS O14964 | 3 | EBI-10192648, EBI-740220 | |
BINARY | O95954 | KASH5 Q8N6L0 | 3 | EBI-10192648, EBI-749265 | |
BINARY | O95954 | MED4 Q9NPJ6 | 3 | EBI-10192648, EBI-394607 | |
BINARY | O95954 | PALS1 Q8N3R9 | 3 | EBI-10192648, EBI-2513978 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-181 | Formiminotransferase N-subdomain | ||||
Sequence: MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARKF | ||||||
Region | 182-326 | Formiminotransferase C-subdomain | ||||
Sequence: LIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLDFEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRIRLVVSRLGLDSLCPFSPKERIIEYLV | ||||||
Region | 327-334 | Linker | ||||
Sequence: PERGPERG | ||||||
Region | 335-541 | Cyclodeaminase/cyclohydrolase | ||||
Sequence: LGSKSLRAFVGEVGARSAAPGGGSVAAAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYLEAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDLQVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQE |
Sequence similarities
In the C-terminal section; belongs to the cyclodeaminase/cyclohydrolase family.
In the N-terminal section; belongs to the formiminotransferase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O95954-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameA
- Length541
- Mass (Da)58,927
- Last updated2000-05-30 v2
- ChecksumC6CFEBFC6DC2ED68
O95954-2
- NameC
- Differences from canonical
- 514-541: IHHRVSSLLQEAKTQAALVLDCLETRQE → PPAGSQDPGCTGAGLLGDPAGVTVREASPGSVAPPSPIPRGQSCDLETPGTAGPSTLEG
O95954-3
- NameD
- Differences from canonical
- 421-541: EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDLQVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQE → AHGGPTGGSEAGSLCAADAGGDGGLAVAGAAGTGPVWEPGLPVRPPGGGQSPGDGRVWRIFQRAHQPEGHHRRGI
O95954-4
- NameE
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q49AR5 | Q49AR5_HUMAN | FTCD | 53 | ||
A0A0G2JQF2 | A0A0G2JQF2_HUMAN | FTCD | 420 | ||
A0A804HKA5 | A0A804HKA5_HUMAN | FTCD | 119 | ||
H7C315 | H7C315_HUMAN | FTCD | 133 | ||
B7WPK3 | B7WPK3_HUMAN | FTCD | 495 |
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_004257 | 123-158 | in isoform E | |||
Sequence: VYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADW → GLTAGLSCSLPVRRGSQDGQSPDPAGHPGRGVRGPP | ||||||
Alternative sequence | VSP_004258 | 159-541 | in isoform E | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_004259 | 421-541 | in isoform D | |||
Sequence: EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDLQVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQE → AHGGPTGGSEAGSLCAADAGGDGGLAVAGAAGTGPVWEPGLPVRPPGGGQSPGDGRVWRIFQRAHQPEGHHRRGI | ||||||
Alternative sequence | VSP_004260 | 514-541 | in isoform C | |||
Sequence: IHHRVSSLLQEAKTQAALVLDCLETRQE → PPAGSQDPGCTGAGLLGDPAGVTVREASPGSVAPPSPIPRGQSCDLETPGTAGPSTLEG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF169017 EMBL· GenBank· DDBJ | AAF15558.1 EMBL· GenBank· DDBJ | mRNA | ||
AF289021 EMBL· GenBank· DDBJ | AAG01852.1 EMBL· GenBank· DDBJ | mRNA | ||
AF289022 EMBL· GenBank· DDBJ | AAG01853.1 EMBL· GenBank· DDBJ | mRNA | ||
AF289023 EMBL· GenBank· DDBJ | AAG01854.1 EMBL· GenBank· DDBJ | mRNA | ||
AF289024 EMBL· GenBank· DDBJ | AAG01855.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052248 EMBL· GenBank· DDBJ | AAH52248.2 EMBL· GenBank· DDBJ | mRNA | ||
BC136383 EMBL· GenBank· DDBJ | AAI36384.1 EMBL· GenBank· DDBJ | mRNA | ||
BC136395 EMBL· GenBank· DDBJ | AAI36396.1 EMBL· GenBank· DDBJ | mRNA | ||
U91541 EMBL· GenBank· DDBJ | AAD15627.1 EMBL· GenBank· DDBJ | mRNA |