Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P53603

- FTCD_PIG

UniProt

P53603 - FTCD_PIG

Protein

Formimidoyltransferase-cyclodeaminase

Gene

FTCD

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Pyridoxal phosphate.

    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

    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. centriole Source: UniProtKB-SubCell
    2. Golgi apparatus Source: UniProtKB-SubCell

    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 – 74
    Beta strandi10 – 123
    Helixi17 – 2812
    Beta strandi34 – 418
    Turni42 – 454
    Beta strandi46 – 538
    Helixi55 – 7218
    Helixi75 – 773
    Beta strandi85 – 9814
    Helixi101 – 11919
    Beta strandi123 – 1275
    Helixi133 – 1353
    Helixi138 – 1425
    Helixi145 – 1528
    Helixi156 – 1583
    Beta strandi161 – 1633
    Turni169 – 1713
    Beta strandi174 – 1785
    Beta strandi183 – 1919
    Helixi193 – 20311
    Beta strandi219 – 2268
    Turni227 – 2304
    Beta strandi231 – 2399
    Turni241 – 2433
    Helixi246 – 25914
    Beta strandi264 – 2718
    Helixi275 – 28915
    Helixi296 – 30712
    Turni308 – 3103
    Beta strandi311 – 3133
    Helixi317 – 3204
    Helixi322 – 3254

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSQLVECVPN FSEGKNQEVI DAISRAVAQT PGCVLLDVDS GPSTNRTVYT    50
    FVGRPEDVVE GALNAARAAY QLIDMSRHHG EHPRMGALDV CPFIPVRGVT 100
    MDECVRCAQA FGQRLAEELG VPVYLYGEAA RTAGRQSLPA LRAGEYEALP 150
    EKLKQAEWAP DFGPSAFVPS WGATVAGARK FLLAFNINLL STREQAHRIA 200
    LDLREQGRGK DQPGRLKKVQ AIGWYLDEKN LAQVSTNLLD FEVTGLHTVF 250
    EETCREAQEL SLPVVGSQLV GLVPLKALLD AAAFYCEKEN LFLLQDEHRI 300
    RLVVNRLGLD SLAPFKPKER IIEYLVPEAG PEQSLLHKPL RTFVREVGSR 350
    SAAPGAGSVA AATAAMGAAL ASMVGLMTYG RRQFEHLDAT MRRLIPPFHA 400
    ASAKLTSLVD ADARAFEAYL KAMKLPKDTP EDKDRRAAAL QEGLRQAVAV 450
    PLALAETVAS LWPALQELAL CGNLACRSDL QVAAKALETG VFGAYFNVLI 500
    NLKDVTDDAF KAQVRQRISS LLQEAKTQAA LVLDRLEARQ A 541
    Length:541
    Mass (Da):58,930
    Last modified:October 1, 1996 - v1
    Checksum:iD52974A9EE088DDF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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: October 1, 2014
    This is version 99 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