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Q5M4U2 (FTHS_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formate--tetrahydrofolate ligase

EC=6.3.4.3
Alternative name(s):
Formyltetrahydrofolate synthetase
Short name=FHS
Short name=FTHFS
Gene names
Name:fhs
Ordered Locus Names:stu0791
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Sequence similarities

Belongs to the formate--tetrahydrofolate ligase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfolic acid-containing compound biosynthetic process

Inferred from electronic annotation. Source: InterPro

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

formate-tetrahydrofolate ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000199399

Regions

Nucleotide binding65 – 728ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M4U2 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: EE071D3138357CCA

FASTA55659,778
        10         20         30         40         50         60 
MKTDIEIAQS VELKPITEVV EKVGIGFDDL ELYGKYKAKL SFDKINEVKD DKPGKLILVT 

        70         80         90        100        110        120 
AINPTPAGEG KSTISIGLAD ALNKIGKKTM IALREPSLGP VMGIKGGAAG GGYAQVLPME 

       130        140        150        160        170        180 
DINLHFTGDM HAITTANNAL SALLDNHIHQ GNALGIDQRR IIWKRVVDLN DRALRHVTVG 

       190        200        210        220        230        240 
LGGPLNGIPR EDGFDITVAS EIMAILCLAT DINDLKERLA NIVVAYRYDR TPVYVRDLEI 

       250        260        270        280        290        300 
EGALTLILKD AIKPNLVQTI YGTPALVHGG PFANIAHGCN SVLATSTALR LADYTVTEAG 

       310        320        330        340        350        360 
FGADLGAEKF LDIKTPNLPT TPDAVVIVAT LRALKMHGGV AKTDLSEENV QAVRDGFSNL 

       370        380        390        400        410        420 
KRHVENIRKF GIPVVVAINE FVADTEAEIA ALKELCSEIK VPVELASVWA NGADGGIDLA 

       430        440        450        460        470        480 
NTVVDVVENG NADYKRLYSD DDSLEEKITK IVTEIYGGKS VVFEKKAKNQ LKQFAEFGWD 

       490        500        510        520        530        540 
KLPVCMAKTQ YSFSDNQFLL GAPEGFDITI REFVPKTGAG FIVALTGDVM TMPGLPKAPA 

       550 
ALKMDVTEDG TAVGLF 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV60470.1.
RefSeqYP_139285.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M4U2.
SMRQ5M4U2. Positions 4-554.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264199.stu0791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV60470; AAV60470; stu0791.
GeneID3164606.
KEGGstl:stu0791.
PATRIC19803163. VBIStrThe97850_0787.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2759.
HOGENOMHOG000040280.
KOK01938.
OMACGEIMTM.
OrthoDBEOG6PCPSP.
ProtClustDBPRK13505.

Enzyme and pathway databases

BioCycSTHE264199:GI6K-809-MONOMER.
UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_01543. FTHFS.
InterProIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF01268. FTHFS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFTHS_STRT2
AccessionPrimary (citable) accession number: Q5M4U2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways