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Protein

Formate--tetrahydrofolate ligase

Gene

THFS

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 858ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • copper ion binding Source: TAIR
  • formate-tetrahydrofolate ligase activity Source: UniProtKB-EC

GO - Biological processi

  • folic acid-containing compound biosynthetic process Source: InterPro
  • response to cadmium ion Source: TAIR
  • response to cytokinin Source: TAIR
  • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G50480-MONOMER.
ReactomeiREACT_297985. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Formate--tetrahydrofolate ligase (EC:6.3.4.3)
Alternative name(s):
10-formyletrahydrofolate synthetase
Short name:
FHS
Short name:
FTHFS
Formyltetrahydrofolate synthetase
Gene namesi
Name:THFS
Ordered Locus Names:At1g50480
ORF Names:F11F12.17, F17J6.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G50480.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 634634Formate--tetrahydrofolate ligasePRO_0000199417Add
BLAST

Proteomic databases

PaxDbiQ9SPK5.
PRIDEiQ9SPK5.

2D gel databases

World-2DPAGE0003:Q9SPK5.

Expressioni

Gene expression databases

GenevestigatoriQ9SPK5.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9SPK5. 1 interaction.
STRINGi3702.AT1G50480.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SPK5.
SMRiQ9SPK5. Positions 14-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2759.
HOGENOMiHOG000040280.
InParanoidiQ9SPK5.
KOiK01938.
OMAiHEYLDEN.
PhylomeDBiQ9SPK5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01543. FTHFS.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SPK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSTRKLEV VSPVPADIDI ANSVEPLHIS EIAKDLNINP LHYDLYGKYK
60 70 80 90 100
AKVLLSAFDE LQGQEDGYYV VVGGITPTPL GEGKSTTTVG LCQALGAYLD
110 120 130 140 150
KKVVTCLRQP SQGPTFGIKG GAAGGGYSQV IPMDEFNLHL TGDIHAITAS
160 170 180 190 200
NNLLAAAIDT RIFHETSQSD KALFNRLCPP NKEGKRSFSD IMFRRLTKLG
210 220 230 240 250
ISKTSPEELT PEEIKKFARL DIDPASITWR RVMDVNDRFL RKITIGQGPE
260 270 280 290 300
EKGMTRETGF DISVASEIMA VLALTTSLGD MRERLGKMVI GNSKAGDPIT
310 320 330 340 350
ADDLGVGGAL TVLMKDAINP TLMQTLEGTP VLVHAGPFAN IAHGNSSIVA
360 370 380 390 400
DKIALKLVGP GGFVVTEAGF GSDIGTEKFM NIKCRYSGLT PQCAIVVATV
410 420 430 440 450
RALKMHGGGP DVVAGRPLDR AYVSENVSLV EAGCVNLAKH ISNTKAYGVN
460 470 480 490 500
VIVAVNMFAT DTEAELNAVR KFSMDAGAFD AVVCSHHAHS GKGAVDLGIA
510 520 530 540 550
VEKACQNITQ PLRFLYPLDI GIKDKIEAIA KSYGASGVEY SDQAEKQIEM
560 570 580 590 600
YTQQGFSNLP ICMSKTQYSF SHDASKKGAP SGFVLPIRDV RGSIGAGFIY
610 620 630
PLVGTMSTMP GLPTRPCFYE IDIDTETGKV RGLS
Length:634
Mass (Da):67,802
Last modified:May 1, 2000 - v1
Checksum:i5BD9D10603D2FF9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162279 mRNA. Translation: AAD56290.1.
AC012561 Genomic DNA. Translation: AAF87882.1.
AC079279 Genomic DNA. Translation: AAG51185.1.
CP002684 Genomic DNA. Translation: AEE32555.1.
AY054637 mRNA. Translation: AAK96828.1.
AY081549 mRNA. Translation: AAM10111.1.
PIRiC96541.
RefSeqiNP_564571.1. NM_103931.3.
UniGeneiAt.21610.
At.71081.

Genome annotation databases

EnsemblPlantsiAT1G50480.1; AT1G50480.1; AT1G50480.
GeneIDi841470.
KEGGiath:AT1G50480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF162279 mRNA. Translation: AAD56290.1.
AC012561 Genomic DNA. Translation: AAF87882.1.
AC079279 Genomic DNA. Translation: AAG51185.1.
CP002684 Genomic DNA. Translation: AEE32555.1.
AY054637 mRNA. Translation: AAK96828.1.
AY081549 mRNA. Translation: AAM10111.1.
PIRiC96541.
RefSeqiNP_564571.1. NM_103931.3.
UniGeneiAt.21610.
At.71081.

3D structure databases

ProteinModelPortaliQ9SPK5.
SMRiQ9SPK5. Positions 14-633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9SPK5. 1 interaction.
STRINGi3702.AT1G50480.1-P.

2D gel databases

World-2DPAGE0003:Q9SPK5.

Proteomic databases

PaxDbiQ9SPK5.
PRIDEiQ9SPK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G50480.1; AT1G50480.1; AT1G50480.
GeneIDi841470.
KEGGiath:AT1G50480.

Organism-specific databases

GeneFarmi4946.
TAIRiAT1G50480.

Phylogenomic databases

eggNOGiCOG2759.
HOGENOMiHOG000040280.
InParanoidiQ9SPK5.
KOiK01938.
OMAiHEYLDEN.
PhylomeDBiQ9SPK5.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciARA:AT1G50480-MONOMER.
ReactomeiREACT_297985. Metabolism of folate and pterines.

Miscellaneous databases

PROiQ9SPK5.

Gene expression databases

GenevestigatoriQ9SPK5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01543. FTHFS.
InterProiIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01268. FTHFS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA encoding 10-formyletrahydrofolate synthetase from Arabidopsis thaliana."
    Skavdahl M., Olson B.J.S.C., Markwell J., Osterman J.C.
    Plant Gene Register PGR99-133
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Hypocotyl.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiFTHS_ARATH
AccessioniPrimary (citable) accession number: Q9SPK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.