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A4J0S6 (FTHS_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Dred_0129
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length567 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 – 567567Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000333314

Regions

Nucleotide binding68 – 758ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4J0S6 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 246CA1784F2A0B40

FASTA56760,771
        10         20         30         40         50         60 
MKKVPSDLEI AQAHEMIPIA EIAKNIGLGE DDIDLYGKYK AKISLDVLRK FNDRAMGKLI 

        70         80         90        100        110        120 
DITAITPTPL GEGKTVTTIG LCQGLGKIGK KVITTLRQPS MGPVFGIKGG AAGGGYSQVV 

       130        140        150        160        170        180 
PMEDINIHFT GDIHAVEAAN NLLAAMIDTS ILLGNPLNID PMTVMWNRVL DTNDRALRDI 

       190        200        210        220        230        240 
VVGLGGKENG YPRQTSFDMA VASEVMAILA LAENLHDLRQ RLGRIIVAYT YDGKPVTAED 

       250        260        270        280        290        300 
LKAAGAMTVI MKEALKPNLV QTLEGQACIM HAGPFANIAH GNNSVLADKI ALNLADYVVT 

       310        320        330        340        350        360 
ESGFGSDLGM EKFMDIKCRQ SGLRPSCVVI TCTIRALKMH GGLGNVVAGK PLPEELTREN 

       370        380        390        400        410        420 
LPALEKGCAN LAHHIKVASY YGVPVVVSIN RFTPDTDAEV DLVRKKALEA GALGAYPITV 

       430        440        450        460        470        480 
WAEGGEGAIE LAEAVVAACE KTADFQLLYP DNLSIKEKIE VLATKVYNAD GVVFEPLAER 

       490        500        510        520        530        540 
KIKQFEDLGL GHLPICMAKT HLSISHDPAM KGLPKNYIFP IRDIRASVGA GFLYPLAGAM 

       550        560 
RTMPGLGSKP AAHNVDIDEY GRTVGLF 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO48679.1.
RefSeqYP_001111504.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J0S6.
SMRA4J0S6. Positions 7-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349161.Dred_0129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO48679; ABO48679; Dred_0129.
GeneID4958473.
KEGGdrm:Dred_0129.
PATRIC21726028. VBIDesRed82656_0137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2759.
HOGENOMHOG000040280.
KOK01938.
OMACIMHAGP.
OrthoDBEOG6PCPSP.

Enzyme and pathway databases

BioCycDRED349161:GHP6-142-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_DESRM
AccessionPrimary (citable) accession number: A4J0S6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 2007
Last modified: May 14, 2014
This is version 46 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