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Protein

5-formyltetrahydrofolate cyclo-ligase

Gene

FAU1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Only enzyme known to utilize 5-formyltetrahydrofolate (folinic acid) as substrate. Contributes to tetrahydrofolate metabolism in an alternative way of folate biosynthesis. May regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids.1 Publication

Catalytic activityi

ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate.1 Publication

Kineticsi

  1. KM=43 µM for ATP1 Publication
  2. KM=33 µM for 5-formyltetrahydrofolate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561SubstrateBy similarity
    Binding sitei194 – 1941ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 85ATPBy similarity
    Nucleotide bindingi151 – 1588ATPBy similarity

    GO - Molecular functioni

    • 5-formyltetrahydrofolate cyclo-ligase activity Source: SGD
    • ATP binding Source: UniProtKB-KW

    GO - Biological processi

    • folic acid-containing compound biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YER183C-MONOMER.
    SABIO-RKP40099.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-formyltetrahydrofolate cyclo-ligase (EC:6.3.3.2)
    Alternative name(s):
    5,10-methenyl-tetrahydrofolate synthetase
    Short name:
    MTHFS
    Short name:
    Methenyl-THF synthetase
    Gene namesi
    Name:FAU1
    Ordered Locus Names:YER183C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome V

    Organism-specific databases

    CYGDiYER183c.
    EuPathDBiFungiDB:YER183C.
    SGDiS000000985. FAU1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    Abolishes methenyltetrahydrofolate synthase activity and leads to accumulation of folinic acid. Leads to a striking methionine deficiency when combined with ADE16 and ADE17, 2 isoenzymes involved in the purine synthesis.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2112115-formyltetrahydrofolate cyclo-ligasePRO_0000200280Add
    BLAST

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP40099.
    PaxDbiP40099.

    Interactioni

    Protein-protein interaction databases

    BioGridi36937. 19 interactions.
    IntActiP40099. 1 interaction.
    MINTiMINT-4484715.

    Structurei

    3D structure databases

    ProteinModelPortaliP40099.
    SMRiP40099. Positions 26-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 1565Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0212.
    GeneTreeiENSGT00390000017791.
    HOGENOMiHOG000007299.
    InParanoidiP40099.
    KOiK01934.
    OMAiSCYLSMP.
    OrthoDBiEOG7FBRWF.

    Family and domain databases

    Gene3Di3.40.50.10420. 1 hit.
    InterProiIPR002698. FTHF_cligase.
    IPR024185. FTHF_cligase-like.
    [Graphical view]
    PANTHERiPTHR23407:SF1. PTHR23407:SF1. 1 hit.
    PfamiPF01812. 5-FTHF_cyc-lig. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006806. FTHF_cligase. 1 hit.
    TIGRFAMsiTIGR02727. MTHFS_bact. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P40099-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATKQLLRRQ IKRVINALDY DIIAAESHTI SQAVRSLIAS ANSRRVACYM
    60 70 80 90 100
    SMDKGEVTTG EIIKNLFQDG QEVFLPRCTH TSESKHFKLR EDHHPHLIFH
    110 120 130 140 150
    RMSSLKMVRD LKPQGPYQLK EPEPHIEESD ILDVVLVPGV AFDIKTGARM
    160 170 180 190 200
    GHGAGYYDDF FQRYKILHEG QKPLLVGLCL MEQVASPIPL EKHDYSMDCI
    210
    VCGDGSIHWF Q
    Length:211
    Mass (Da):24,059
    Last modified:February 1, 1995 - v1
    Checksum:i96F0D84B3B69DD57
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18922 Genomic DNA. Translation: AAB64710.1.
    BK006939 Genomic DNA. Translation: DAA07846.1.
    PIRiS50686.
    RefSeqiNP_011110.1. NM_001179073.1.

    Genome annotation databases

    EnsemblFungiiYER183C; YER183C; YER183C.
    GeneIDi856932.
    KEGGisce:YER183C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18922 Genomic DNA. Translation: AAB64710.1.
    BK006939 Genomic DNA. Translation: DAA07846.1.
    PIRiS50686.
    RefSeqiNP_011110.1. NM_001179073.1.

    3D structure databases

    ProteinModelPortaliP40099.
    SMRiP40099. Positions 26-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36937. 19 interactions.
    IntActiP40099. 1 interaction.
    MINTiMINT-4484715.

    Proteomic databases

    MaxQBiP40099.
    PaxDbiP40099.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYER183C; YER183C; YER183C.
    GeneIDi856932.
    KEGGisce:YER183C.

    Organism-specific databases

    CYGDiYER183c.
    EuPathDBiFungiDB:YER183C.
    SGDiS000000985. FAU1.

    Phylogenomic databases

    eggNOGiCOG0212.
    GeneTreeiENSGT00390000017791.
    HOGENOMiHOG000007299.
    InParanoidiP40099.
    KOiK01934.
    OMAiSCYLSMP.
    OrthoDBiEOG7FBRWF.

    Enzyme and pathway databases

    BioCyciYEAST:YER183C-MONOMER.
    SABIO-RKP40099.

    Miscellaneous databases

    NextBioi983412.
    PROiP40099.

    Family and domain databases

    Gene3Di3.40.50.10420. 1 hit.
    InterProiIPR002698. FTHF_cligase.
    IPR024185. FTHF_cligase-like.
    [Graphical view]
    PANTHERiPTHR23407:SF1. PTHR23407:SF1. 1 hit.
    PfamiPF01812. 5-FTHF_cyc-lig. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006806. FTHF_cligase. 1 hit.
    TIGRFAMsiTIGR02727. MTHFS_bact. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Cloning and characterization of methenyltetrahydrofolate synthetase from Saccharomyces cerevisiae."
      Holmes W.B., Appling D.R.
      J. Biol. Chem. 277:20205-20213(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    6. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
      Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
      Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFTHC_YEAST
    AccessioniPrimary (citable) accession number: P40099
    Secondary accession number(s): D3DM92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: July 22, 2015
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 468 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3

    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 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.