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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

  1. 5-formyltetrahydrofolate cyclo-ligase activity Source: SGD
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. 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

  1. Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
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.

Expressioni

Gene expression databases

GenevestigatoriP40099.

Interactioni

Protein-protein interaction databases

BioGridi36937. 19 interactions.
IntActiP40099. 1 interaction.
MINTiMINT-4484715.
STRINGi4932.YER183C.

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.
STRINGi4932.YER183C.

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.

Gene expression databases

GenevestigatoriP40099.

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: April 29, 2015
This is version 109 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.