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Q8NZ49 (FTHS2_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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 2

EC=6.3.4.3
Alternative name(s):
Formyltetrahydrofolate synthetase 2
Short name=FHS 2
Short name=FTHFS 2
Gene names
Name:fhs2
Ordered Locus Names:spyM18_2144
OrganismStreptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]
Taxonomic identifier186103 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length557 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 – 557557Formate--tetrahydrofolate ligase 2 HAMAP-Rule MF_01543
PRO_0000199392

Regions

Nucleotide binding66 – 738ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NZ49 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 7A7222A02BD5A804

FASTA55759,054
        10         20         30         40         50         60 
MVLSDIEIAN SVTMEPISKV ANQLGIDEEA LCLYGKYKAK IDARQLVALK DKPDGKLILV 

        70         80         90        100        110        120 
TAISPTPAGE GKTTTSVGLV DALSAIGKKA VIALREPSLG PVFGVKGGAA GGGHAQVVPM 

       130        140        150        160        170        180 
EDINLHFTGD FHAIGVANNL LAALIDNHIH HGNSLGIDSR RITWKRVVDM NDRQLRHIVD 

       190        200        210        220        230        240 
GLQGKVNGVP REDGYDITVA SEIMAILCLS ENISDLKARL EKIIIGYNYQ GEPVTAKDLK 

       250        260        270        280        290        300 
AGGALAALLK DAIHPNLVQT LEHTPALIHG GPFANIAHGC NSVLATKLAL KYGDYAVTEA 

       310        320        330        340        350        360 
GFGADLGAEK FIDIKCRMSG LRPAAVVLVA TIRALKMHGG VPKADLATEN VQAVVDGLPN 

       370        380        390        400        410        420 
LDKHLANIQD VYGLPVVVAI NKFPLDTDAE LQAVYDACDK RGVDVVISDV WANGGAGGRE 

       430        440        450        460        470        480 
LAEKVVALAE QDNQFCFVYE EDDSIETKLT KIVTKVYGGK GIRLTPAAKR ELADLERLSF 

       490        500        510        520        530        540 
GNYPICMAKT QYSFSDDAKK LGAPTDFTVT ISNLKVSAGA GFIVALTGAI MTMPGLPKVP 

       550 
ASETIDIDEE GNITGLF 

« Hide

References

[1]"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009949 Genomic DNA. Translation: AAL98593.1.
RefSeqNP_608094.1. NC_003485.1.

3D structure databases

ProteinModelPortalQ8NZ49.
SMRQ8NZ49. Positions 5-555.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186103.spyM18_2144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL98593; AAL98593; spyM18_2144.
GeneID994232.
KEGGspm:spyM18_2144.
PATRIC19750694. VBIStrPyo4396_1911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2759.
HOGENOMHOG000040280.
KOK01938.
OMAQLRYIND.
OrthoDBEOG6PCPSP.

Enzyme and pathway databases

BioCycSPYO186103:GHJG-1833-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 nameFTHS2_STRP8
AccessionPrimary (citable) accession number: Q8NZ49
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 68 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