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P28723 (FTHS_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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):
10-formyletrahydrofolate synthetase
Short name=FHS
Short name=FTHFS
Formyltetrahydrofolate synthetase
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Homodimer.

Sequence similarities

Belongs to the formate--tetrahydrofolate ligase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 637636Formate--tetrahydrofolate ligase HAMAP-Rule MF_01543
PRO_0000199418

Regions

Nucleotide binding81 – 888ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P28723 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AAF08ABA23C54B9E

FASTA63767,855
        10         20         30         40         50         60 
MGGSSKTVRK LEVATPVPAD IDIANAVEPL HIADIAADLN LSPRHYDLYG KYKAKVLLSV 

        70         80         90        100        110        120 
LDEVQETQDG YYVVVGGITP TPLGEGKSTT TVGLCQALGA FLDKKVVTCL RQPSQGPTFG 

       130        140        150        160        170        180 
IKGGAAGGGY SQVIPMDEFN LHLTGDIHAI TASNNLLAAA IDTRMFHEST QSDKALFNRL 

       190        200        210        220        230        240 
CPPNKEGKRT FCNIMHRRLK KLGIDKTNPD DLTPEEVTKF ARLDIDPDSI TWRRVMDVND 

       250        260        270        280        290        300 
RFLRKISVGQ GPDEKGMVRE TGFDISVASE IMAVLALTTS LADMRERLGK MVIGNSKAGE 

       310        320        330        340        350        360 
PITADDLGLG GALTVLMKDA INPTLMQTLE GTPVLVHAGP FANIAHGNSS IVADKIALKL 

       370        380        390        400        410        420 
VGPGGFVVTE AGFGSDIGTE KFMNIKCRYS GLTPQCAIVV ATVRALKMHG GGPQVVAGKP 

       430        440        450        460        470        480 
LDRAYLTENV GLVEAGCVNL ARHIINTKAY GSNVVVAINM FSSDTEAELN AVKKAAMDAG 

       490        500        510        520        530        540 
AFDAVICTHH AHGGKGAVDL GIAVQKACEN VTQPLRFLYP LDISIKEKIE AIAKSYGAAG 

       550        560        570        580        590        600 
VEYSEQAEKK IEMYSKQGFS NLPICMAKTQ YSFSHNAAEK GAPSGFILPI RDVRGSIGAG 

       610        620        630 
FIYPLVGTMS TMPGLPTRPC FFDIDLDTTT GKVIGLS 

« Hide

References

[1]"Isolation and sequencing of the cDNA coding for spinach 10-formyltetrahydrofolate synthetase. Comparisons with the yeast, mammalian, and bacterial proteins."
Nour J.M., Rabinowitz J.C.
J. Biol. Chem. 267:16292-16296(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation, characterization, and structural organization of 10-formyltetrahydrofolate synthetase from spinach leaves."
Nour J.M., Rabinowitz J.C.
J. Biol. Chem. 266:18363-18369(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-36.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83940 mRNA. Translation: AAA34046.1.
PIRA40948.
A43350.

3D structure databases

ProteinModelPortalP28723.
SMRP28723. Positions 170-233.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP28723.
ProMEXP28723.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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. 2 hits.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFTHS_SPIOL
AccessionPrimary (citable) accession number: P28723
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 61 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways