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Q98HQ4 (FTHS_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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:mlr2763
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

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.

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_0000199371

Regions

Nucleotide binding68 – 758ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98HQ4 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 28FD5270D2672978

FASTA55959,971
        10         20         30         40         50         60 
MAEVKSDIEI ARAAKKKQIQ EIGQKIGIPT EHLLPYGHDK AKISAEFIKS VKGNKDGKLI 

        70         80         90        100        110        120 
LVTAINPTPA GEGKTTTTVG LGDGLNRIGK KAIVCIREAS LGPNFGVKGG AAGGGYAQVV 

       130        140        150        160        170        180 
PMEDMNLHFT GDFHAITTAH NLLSALIDNH IYWGNELGID TRRVVWRRVM DMNDRALREM 

       190        200        210        220        230        240 
ICSLGGVANG FPREGGFDIT VASEVMAILC LSTDLKDLEK RLGDIIVAYR RDKSPVYARD 

       250        260        270        280        290        300 
LKADGAMAVL LKDAMQPNLV QTLENNPAFV HGGPFANIAH GCNSVVATTT ALKLADYVVT 

       310        320        330        340        350        360 
EAGFGADLGA EKFFDIKCRK AGLKPAAAVI VATVRAMKMN GGVKKEDLGK ENIEAVKKGC 

       370        380        390        400        410        420 
ANLGRHIENI RQFGVPAVVA INHFYSDTDA EIQAMKDYVA SMGEEAVLCK HWAKGSAGIE 

       430        440        450        460        470        480 
ELANKVVALA ESGASQFAPL YPDAMPLFEK INTIVQRIYR GSEAIADKSV RDQLHAWEQA 

       490        500        510        520        530        540 
GYGNLPVCMA KTQYSFSTDP NLRGAPTGHT VPVREVRLSA GAGFVVIICG EVMTMPGLPK 

       550 
APSSEKIFLN EAGQIEGLF 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB49812.1.
RefSeqNP_104026.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98HQ4.
SMRQ98HQ4. Positions 7-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr2763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB49812; BAB49812; BAB49812.
GeneID1226687.
KEGGmlo:mlr2763.
PATRIC22478611. VBIMesLot2464_2212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-2150-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_RHILO
AccessionPrimary (citable) accession number: Q98HQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 63 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