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Q1GA94 (FTHS_LACDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Ldb1020
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]
Taxonomic identifier390333 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length559 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.

Sequence caution

The sequence CAI97822.1 differs from that shown. Reason: Erroneous initiation.

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 – 559559Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000293039

Regions

Nucleotide binding67 – 748ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GA94 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 750ABAED922A5D41

FASTA55960,503
        10         20         30         40         50         60 
MVKSDIEIAQ AAEELPITDV AAKLGLTSQD LEPYGYDKAK VNWQAIKRSE ENGHLGKLIL 

        70         80         90        100        110        120 
VTSISPTPAG EGKSTMTIGI GDAINNQLGK KTVIALREPS MGPVFGMKGG AAGGGYAQVI 

       130        140        150        160        170        180 
PMEDINLHFT GDMHALTSAI DNLSALVDNY IYQGNELGLD PEKIVIKRGL DVNDRTLRKV 

       190        200        210        220        230        240 
TIGQGSKFNG VERPASFQLT VGHELMAILC LSKDIADLKE RIGKVLVGYT YEDEPVFVKD 

       250        260        270        280        290        300 
LGFQGAIAAL LSTALKPNLV QTLEHTPAFV HGGPFANIAH GNNSILSTNL ALHLSDYVLS 

       310        320        330        340        350        360 
EAGFGSDLGG QKFLDFVSTK LEKKPDAAVV VATVRALKYQ AEKSTDHLKE ENLDSLKEGF 

       370        380        390        400        410        420 
ANLDRHMNNV RSYNIPVLVV INKFPTDTEA ELDLLKSLIE EQGFPCEIVT AHDEGSKGAK 

       430        440        450        460        470        480 
AAAEKIVELA DKSDYEIKRS YDLDDDLETK IEKVAKRIYH AADVEYTDKA KDQLVKLKKM 

       490        500        510        520        530        540 
GKDKLPVIIA KTQYSFTDNV KELGAPTGFT LHVKGLSLRN GAGFVVVSTG HILDMPGLPK 

       550 
HPAALDIDVD ETGKISGLF 

« Hide

References

[1]"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution."
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. expand/collapse author list , Weissenbach J., Ehrlich S.D., Maguin E.
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11842 / DSM 20081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954253 Genomic DNA. Translation: CAI97822.1. Different initiation.
RefSeqYP_618996.2. NC_008054.1.

3D structure databases

ProteinModelPortalQ1GA94.
SMRQ1GA94. Positions 5-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390333.Ldb1020.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI97822; CAI97822; Ldb1020.
GeneID4083928.
KEGGldb:Ldb1020.
PATRIC22217609. VBILacDel123523_0923.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2759.
HOGENOMHOG000040280.
KOK01938.
OrthoDBEOG6PCPSP.

Enzyme and pathway databases

BioCycLDEL390333:GIXG-1008-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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFTHS_LACDA
AccessionPrimary (citable) accession number: Q1GA94
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 50 of the entry and version 2 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