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P80405

- MTHFS_RABIT

UniProt

P80405 - MTHFS_RABIT

Protein

5-formyltetrahydrofolate cyclo-ligase

Gene

MTHFS

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    Magnesium.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

    1. 5-formyltetrahydrofolate cyclo-ligase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. folic acid binding Source: UniProtKB-KW

    GO - Biological processi

    1. folic acid-containing compound biosynthetic process Source: InterPro
    2. tetrahydrofolate metabolic process Source: UniProtKB

    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: Unplaced

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000023444.

    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.

    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

    AAAAAVSGAK RSLRAELKQR LRAISAEERL RCQRLLTQKV IAHRQYQKSQ    50
    RISIFLSMPD EIETEEIIKD IFQQGKVCFI PRYRLQSNHM DMVKLASADE 100
    ISSLPKTSWN IHQPSESDTR EEALATGGLD LIFMPGLGFD RNGNRLGRGR 150
    GYYDTYLQRC LQQQGAKPYT IALAFREQIC PQVPVDDTDV SVDEVLYVDA 200
    A 201
    Length:201
    Mass (Da):22,733
    Last modified:November 1, 1995 - v1
    Checksum:i6FD20B8D9C31EC46
    GO

    Sequence databases

    PIRiA53688.

    Cross-referencesi

    Sequence databases

    PIRi A53688.

    3D structure databases

    ProteinModelPortali P80405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000023444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG271145.
    HOVERGENi HBG052525.

    Family and domain databases

    Gene3Di 3.40.50.10420. 1 hit.
    InterProi IPR002698. FTHF_cligase.
    IPR024185. FTHF_cligase-like.
    [Graphical view ]
    PANTHERi PTHR23407:SF1. PTHR23407:SF1. 1 hit.
    Pfami PF01812. 5-FTHF_cyc-lig. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006806. FTHF_cligase. 1 hit.
    TIGRFAMsi TIGR02727. MTHFS_bact. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 76 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