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P21164 (FTHS_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismMoorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifier1525 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Subunit structure

Homotetramer. Ref.2

Miscellaneous

Binding of monovalent cations contributes to thermal stability. HAMAP-Rule MF_01543

Sequence similarities

Belongs to the formate--tetrahydrofolate ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000199361

Regions

Nucleotide binding68 – 758ATP By similarity

Secondary structure

1 ................................................................................................................. 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21164 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 36CD2BBB3C909B62

FASTA55959,993
        10         20         30         40         50         60 
MSKVPSDIEI AQAAKMKPVM ELARGLGIQE DEVELYGKYK AKISLDVYRR LKDKPDGKLI 

        70         80         90        100        110        120 
LVTAITPTPA GEGKTTTSVG LTDALARLGK RVMVCLREPS LGPSFGIKGG AAGGGYAQVV 

       130        140        150        160        170        180 
PMEDINLHFT GDIHAVTYAH NLLAAMVDNH LQQGNVLNID PRTITWRRVI DLNDRALRNI 

       190        200        210        220        230        240 
VIGLGGKANG VPRETGFDIS VASEVMACLC LASDLMDLKE RFSRIVVGYT YDGKPVTAGD 

       250        260        270        280        290        300 
LEAQGSMALL MKDAIKPNLV QTLENTPAFI HGGPFANIAH GCNSIIATKT ALKLADYVVT 

       310        320        330        340        350        360 
EAGFGADLGA EKFYDVKCRY AGFKPDATVI VATVRALKMH GGVPKSDLAT ENLEALREGF 

       370        380        390        400        410        420 
ANLEKHIENI GKFGVPAVVA INAFPTDTEA ELNLLYELCA KAGAEVALSE VWAKGGEGGL 

       430        440        450        460        470        480 
ELARKVLQTL ESRPSNFHVL YNLDLSIKDK IAKIATEIYG ADGVNYTAEA DKAIQRYESL 

       490        500        510        520        530        540 
GYGNLPVVMA KTQYSFSDDM TKLGRPRNFT ITVREVRLSA GGRLIVPITG AIMTMPGLPK 

       550 
RPAACNIDID ADGVITGLF

« Hide

References

[1]"Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum."
Lovell C.R., Przybyla A., Ljungdahl L.G.
Biochemistry 29:5687-5694(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica."
Radfar R., Shin R., Sheldrick G.M., Minor W., Lovell C.R., Odom J.D., Dunlap R.B., Lebioda L.
Biochemistry 39:3920-3926(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
[3]"Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica."
Radfar R., Leaphart A., Brewer J.M., Minor W., Odom J.D., Dunlap R.B., Lovell C.R., Lebioda L.
Biochemistry 39:14481-14486(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MONOVALENT CATIONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02911 Genomic DNA. Translation: AAA23240.1.
PIRA35942.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG7X-ray2.50A/B1-559[»]
1FP7X-ray3.20A/B1-559[»]
1FPMX-ray3.00A/B1-559[»]
3QUSX-ray2.84A/B1-559[»]
4JIMX-ray2.20A/B1-559[»]
4JJKX-ray3.00A/B1-559[»]
4JJZX-ray2.50A/B1-559[»]
4JKIX-ray2.67A/B1-559[»]
ProteinModelPortalP21164.
SMRP21164. Positions 7-557.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:FORMYLSYNTHCLTH-MONOMER.
UniPathwayUPA00193.

Family and domain databases

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...

Other

EvolutionaryTraceP21164.

Entry information

Entry nameFTHS_MOOTH
AccessionPrimary (citable) accession number: P21164
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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