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Protein

5-formyltetrahydrofolate cyclo-ligase

Gene

Mthfs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei14ATPBy similarity1
Binding sitei56Substrate; via carbonyl oxygenBy similarity1
Binding sitei61SubstrateBy similarity1
Metal bindingi154MagnesiumBy similarity1
Metal bindingi189MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 14ATPBy similarity5
Nucleotide bindingi145 – 153ATPBy similarity9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi6.3.3.2. 3474.
ReactomeiR-MMU-196757. Metabolism of folate and pterines.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1340032. Mthfs.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrial matrix Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002002762 – 2035-formyltetrahydrofolate cyclo-ligaseAdd BLAST202

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D110.
PaxDbiQ9D110.
PeptideAtlasiQ9D110.
PRIDEiQ9D110.

PTM databases

iPTMnetiQ9D110.
PhosphoSitePlusiQ9D110.

Expressioni

Gene expression databases

BgeeiENSMUSG00000066442.
ExpressionAtlasiQ9D110. baseline and differential.
GenevisibleiQ9D110. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi223657. 2 interactors.
STRINGi10090.ENSMUSP00000082354.

Structurei

3D structure databases

ProteinModelPortaliQ9D110.
SMRiQ9D110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni148 – 152Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3093. Eukaryota.
COG0212. LUCA.
GeneTreeiENSGT00390000017791.
HOGENOMiHOG000007299.
HOVERGENiHBG052525.
InParanoidiQ9D110.
KOiK01934.
OMAiPWVEDKN.
OrthoDBiEOG091G0Q5W.
PhylomeDBiQ9D110.
TreeFamiTF313668.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVTVNSAK RGLRAELKQR LRALSAEERL RQSLLLTQKV IAHNQYQNSK
60 70 80 90 100
RISIFLSMQD EVETEVIIKD IFKQGKICFI PRYQFQSNHM DMVRLTSSEE
110 120 130 140 150
IALLPKTSWN IHQPGEGDVR EEALSTGGLD LIFLPGLGFD KDGNRLGRGK
160 170 180 190 200
GYYDTYLKRC VQHQEVKPYT MALAFKEQIC PQIPVDEHDM KVDEVLYEDS

PAS
Length:203
Mass (Da):23,202
Last modified:January 23, 2007 - v2
Checksum:i4C20DC7416CA5304
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004092 mRNA. Translation: BAB23165.1.
CT030686, AC135634 Genomic DNA. Translation: CAQ52322.1.
CCDSiCCDS23394.1.
RefSeqiNP_081105.1. NM_026829.2.
UniGeneiMm.486274.

Genome annotation databases

EnsembliENSMUST00000085256; ENSMUSP00000082354; ENSMUSG00000066442.
GeneIDi107885.
KEGGimmu:107885.
UCSCiuc009qzk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004092 mRNA. Translation: BAB23165.1.
CT030686, AC135634 Genomic DNA. Translation: CAQ52322.1.
CCDSiCCDS23394.1.
RefSeqiNP_081105.1. NM_026829.2.
UniGeneiMm.486274.

3D structure databases

ProteinModelPortaliQ9D110.
SMRiQ9D110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223657. 2 interactors.
STRINGi10090.ENSMUSP00000082354.

PTM databases

iPTMnetiQ9D110.
PhosphoSitePlusiQ9D110.

Proteomic databases

MaxQBiQ9D110.
PaxDbiQ9D110.
PeptideAtlasiQ9D110.
PRIDEiQ9D110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085256; ENSMUSP00000082354; ENSMUSG00000066442.
GeneIDi107885.
KEGGimmu:107885.
UCSCiuc009qzk.1. mouse.

Organism-specific databases

CTDi10588.
MGIiMGI:1340032. Mthfs.

Phylogenomic databases

eggNOGiKOG3093. Eukaryota.
COG0212. LUCA.
GeneTreeiENSGT00390000017791.
HOGENOMiHOG000007299.
HOVERGENiHBG052525.
InParanoidiQ9D110.
KOiK01934.
OMAiPWVEDKN.
OrthoDBiEOG091G0Q5W.
PhylomeDBiQ9D110.
TreeFamiTF313668.

Enzyme and pathway databases

BRENDAi6.3.3.2. 3474.
ReactomeiR-MMU-196757. Metabolism of folate and pterines.

Miscellaneous databases

PROiQ9D110.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000066442.
ExpressionAtlasiQ9D110. baseline and differential.
GenevisibleiQ9D110. MM.

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...

Entry informationi

Entry nameiMTHFS_MOUSE
AccessioniPrimary (citable) accession number: Q9D110
Secondary accession number(s): B2KF82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.