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Protein

5-formyltetrahydrofolate cyclo-ligase

Gene

MTHFS

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Contributes to tetrahydrofolate metabolism. Helps regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids. Catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-CHO-H4PteGlu) to yield 5,10-methenyltetrahydrofolate. It can also use 5-formyltetrahydropteroic acid (5-CHO-H4Pte) and 5-formyltetrahydropteroylhistidine (5-CHO-H4PteHis) as substrate.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

Kineticsi

Kcat is 2 sec(-1) for cyclo-ligase activity with 5-CHO-H4Pte. Kcat is 3 sec(-1) for cyclo-ligase activity with 5-CHO-H4PteHis. Kcat is 5 sec(-1) for cyclo-ligase activity with 5-CHO-H4PteGlu and 5-CHO-H4PteGlu5.

  1. KM=0.2 µM for 5-CHO-H4PteGlu51 Publication
  2. KM=8 µM for 5-CHO-H4PteGlu1 Publication
  3. KM=11 µM for 5-CHO-H4PteHis1 Publication
  4. KM=21 µM for 5-CHO-H4Pte1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141ATPBy similarity
    Binding sitei56 – 561Substrate; via carbonyl oxygenBy similarity
    Binding sitei61 – 611SubstrateBy similarity
    Metal bindingi154 – 1541MagnesiumBy similarity
    Metal bindingi189 – 1891MagnesiumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 145ATPBy similarity
    Nucleotide bindingi145 – 1539ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Folate-binding, Magnesium, Metal-binding, Nucleotide-binding

    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:MTHFS
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811 Componenti: Unplaced

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2012015-formyltetrahydrofolate cyclo-ligasePRO_0000200277Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP80405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni148 – 1525Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG271145.
    HOVERGENiHBG052525.
    InParanoidiP80405.

    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.

    P80405-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    AAAAAVSGAK RSLRAELKQR LRAISAEERL RCQRLLTQKV IAHRQYQKSQ
    60 70 80 90 100
    RISIFLSMPD EIETEEIIKD IFQQGKVCFI PRYRLQSNHM DMVKLASADE
    110 120 130 140 150
    ISSLPKTSWN IHQPSESDTR EEALATGGLD LIFMPGLGFD RNGNRLGRGR
    160 170 180 190 200
    GYYDTYLQRC LQQQGAKPYT IALAFREQIC PQVPVDDTDV SVDEVLYVDA

    A
    Length:201
    Mass (Da):22,733
    Last modified:November 1, 1995 - v1
    Checksum:i6FD20B8D9C31EC46
    GO

    Sequence databases

    PIRiA53688.

    Cross-referencesi

    Sequence databases

    PIRiA53688.

    3D structure databases

    ProteinModelPortaliP80405.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiNOG271145.
    HOVERGENiHBG052525.
    InParanoidiP80405.

    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

    1. "Primary structure and tetrahydropteroylglutamate binding site of rabbit liver cytosolic 5,10-methenyltetrahydrofolate synthetase."
      Maras B., Stover P., Valiante S., Barra D., Schirch V.
      J. Biol. Chem. 269:18429-18433(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY.
      Tissue: Liver.

    Entry informationi

    Entry nameiMTHFS_RABIT
    AccessioniPrimary (citable) accession number: P80405
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: June 24, 2015
    This is version 80 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    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.