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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

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

GO - Biological processi

  1. tetrahydrofolate metabolic process Source: UniProtKB
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: Unplaced

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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

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.
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...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000023444.

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: January 7, 2015
This is version 79 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.