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Q2LU82 (FTHS_SYNAS) 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:SYNAS_17640
ORF Names:SYN_02008
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length565 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 – 565565Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000293072

Regions

Nucleotide binding65 – 728ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LU82 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: B4CF77DEDE1BFDE1

FASTA56560,940
        10         20         30         40         50         60 
MTHRNSRQDT KELKPIADIA ATIGLSEDDI EAYGRYKAKV RLEAISRFHS RPDASLILVS 

        70         80         90        100        110        120 
AMTPTPAGEG KTTVSIGLAQ ALARLGKATI AALREPSLGP VFGMKGGATG GGLSRVHPVD 

       130        140        150        160        170        180 
DINLHFTNDF AAVESAHNLL SAIVDNSVYH DNILNIDPRK VTWRRVLDMN DRFLRNIVIG 

       190        200        210        220        230        240 
LGGSVNGVPR ETGFDIVPSS EIMAILCLSR SYRELKEKIR RILVGFTYDD SPVMAGDLKV 

       250        260        270        280        290        300 
EGAVTALLKY ALLPNLVQTT ENVPAIIHGG PFANIAQGTS SILGTDLALR LADYVVTEAG 

       310        320        330        340        350        360 
FGFDLGAEKF FDIVAPYGGL NPRIVVLVAT VRALKYHAGI AQADLDRSNP RAAVLGMANL 

       370        380        390        400        410        420 
RKHYQNIDKF HVSCVIALNR FSSDTDEEIN AVVRAAENEG MNIAPCDIFR LGGEGGLELA 

       430        440        450        460        470        480 
EKTLELLAGT SCGYRRLYEW NQPVEDKIFT VASEIYGAVS IDYQPLARRN LDLINKYGFD 

       490        500        510        520        530        540 
KLPVCIAKTQ QSLSDNPGLL GLPRDFIVTV REIRIASGAG FLIPITGEIL RMPGLSKRPA 

       550        560 
AYSIDIDDSG NITGVGSPGG ISSLS 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC77643.1.
RefSeqYP_461811.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LU82.
SMRQ2LU82. Positions 11-554.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_02008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC77643; ABC77643; SYN_02008.
GeneID3882768.
KEGGsat:SYN_02008.
PATRIC23864250. VBISynAci70500_1912.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2759.
HOGENOMHOG000040280.
KOK01938.
OMALKHHGGV.
OrthoDBEOG6PCPSP.

Enzyme and pathway databases

BioCycSACI56780:GHXT-1808-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_SYNAS
AccessionPrimary (citable) accession number: Q2LU82
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 21, 2006
Last modified: May 14, 2014
This is version 50 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