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Q8WZJ7 (C1TC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
C-1-tetrahydrofolate synthase, cytoplasmic

Short name=C1-THF synthase

Including the following 3 domains:

  1. Methylenetetrahydrofolate dehydrogenase
    EC=1.5.1.5
  2. Methenyltetrahydrofolate cyclohydrolase
    EC=3.5.4.9
  3. Formyltetrahydrofolate synthetase
    EC=6.3.4.3
Gene names
ORF Names:SPBC839.16
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH. HAMAP-Rule MF_01543

5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate. HAMAP-Rule MF_01543

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_01543

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01543

Subcellular location

Cytoplasm Ref.2.

Domain

This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity. HAMAP-Rule MF_01543

Sequence similarities

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
Methionine biosynthesis
One-carbon metabolism
Purine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
NADP
Nucleotide-binding
   Molecular functionHydrolase
Ligase
Oxidoreductase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process10-formyltetrahydrofolate biosynthetic process

Inferred from direct assay PubMed 8226914. Source: PomBase

folic acid biosynthetic process

Inferred from direct assay PubMed 8226914. Source: PomBase

histidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

methionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

one-carbon metabolic process

Inferred from direct assay PubMed 8226914. Source: PomBase

purine nucleobase biosynthetic process

Inferred from direct assay PubMed 8226914. Source: PomBase

purine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytosol

Inferred from direct assay Ref.2. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

formate-tetrahydrofolate ligase activity

Inferred from direct assay PubMed 8226914. Source: PomBase

methenyltetrahydrofolate cyclohydrolase activity

Inferred from direct assay PubMed 8226914. Source: PomBase

methylenetetrahydrofolate dehydrogenase (NADP+) activity

Inferred from direct assay PubMed 8226914. Source: PomBase

single-stranded DNA binding

Inferred from direct assay PubMed 8226914. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 937937C-1-tetrahydrofolate synthase, cytoplasmic HAMAP-Rule MF_01543
PRO_0000315626

Regions

Nucleotide binding168 – 1703NADP By similarity
Nucleotide binding374 – 3818ATP By similarity
Region1 – 309309Methylenetetrahydrofolate dehydrogenase and cyclohydrolase HAMAP-Rule MF_01543
Region50 – 545Substrate binding By similarity
Region97 – 993Substrate binding By similarity
Region268 – 2725Substrate binding By similarity
Region310 – 937628Formyltetrahydrofolate synthetase HAMAP-Rule MF_01543

Sites

Binding site1931NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WZJ7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 70FF8700FD023C90

FASTA937101,203
        10         20         30         40         50         60 
MALLLEGTSL ARKVREELRE QISSIKSVDP YFNVSLKIIQ VGGREDSNVY VRMKTRAANE 

        70         80         90        100        110        120 
AGISCEHVNF PEDITEYDLL LAIKGFNEDP TVHGIIVQLP LPAHINEQII TEAVAPEKDV 

       130        140        150        160        170        180 
DGFCETNLGK LTKREGQPLF TACTPKGIMC ILKHYGINVQ GKHAVVIGRS NIVGRPMSIL 

       190        200        210        220        230        240 
LEKANATVTL CHSKTESIAD IVRTADIVVA AIGIPHFVKA DWLKKGVVAI DVGINSIPDA 

       250        260        270        280        290        300 
TKKSGYRLTG DIDFENAKEV ASAITPVPGS VGPMTVAMLL QNVVESAVRF RKMSRKRKPT 

       310        320        330        340        350        360 
LLPLKLQTPV PSDIEIARSQ TPKNIGDLAS EIGIAKSELE FYGSHKAKVN LEILQRLAHR 

       370        380        390        400        410        420 
RDGHYVVVTG ITPTPFGEGK STLTAGLVQA LSNLDKLAIA CVRQPSQGPT FGIKGGAAGG 

       430        440        450        460        470        480 
GYSQFIPMEE FNLHLTGDIH AITAATNLLA AAIDTRMFHE NTQSDAALYK RLTLVKGNKR 

       490        500        510        520        530        540 
EFAPVMFRRL KKLGIDKTNP EELTEEEQRK FARLDIEPST ISWNRTLDVN DRFLRKITIG 

       550        560        570        580        590        600 
ENPTEKGFTR QTGFDLSVAS ECMSVLALAT DLKDMRERLG RMVVASNKSG EPVTADDLGV 

       610        620        630        640        650        660 
GGALTVLLKD AIKPTLMQTL EGTPALVHAG PFANISIGAS SILADRIALK LAGTEVDEDA 

       670        680        690        700        710        720 
KKEAGYVVTE AGFASDIGME KFFNIKCRTS GLKPDAIVIV ATVQALKLHG GGPPVGPGKP 

       730        740        750        760        770        780 
IPEVYKREDV DLVRKGCANL AKHISNARKY GLPVVVAINK FSSDSPNEIS AIREEALAAG 

       790        800        810        820        830        840 
ATDAVDSNHW AEGGKGALGV ARALINACEN VDSEFRLLYD VHEPIEKKIE IIAKEMYGAD 

       850        860        870        880        890        900 
GIELSPLAKE RLETFTKQGY NNLPICIAKT QYSLSHDPDL KGAPTNFTVP IRDMRLSAGA 

       910        920        930 
GFIYPLAAAI STIPGLPTKP AYYNIDIAEN GDIVGLS 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB46709.1.
PIRT40723.
RefSeqNP_595256.1. NM_001021162.2.

3D structure databases

ProteinModelPortalQ8WZJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277731. 2 interactions.
MINTMINT-4700994.
STRING4896.SPBC839.16-1.

Proteomic databases

MaxQBQ8WZJ7.
PaxDbQ8WZJ7.
PRIDEQ8WZJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC839.16.1; SPBC839.16.1:pep; SPBC839.16.
GeneID2541217.
KEGGspo:SPBC839.16.

Organism-specific databases

PomBaseSPBC839.16.

Phylogenomic databases

eggNOGCOG0190.
HOGENOMHOG000040280.
KOK00288.
OMAFAPLMFK.
OrthoDBEOG7K0ZMJ.
PhylomeDBQ8WZJ7.

Enzyme and pathway databases

UniPathwayUPA00193.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProIPR000559. Formate_THF_ligase.
IPR020628. Formate_THF_ligase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR000672. THF_DH/CycHdrlase.
IPR020630. THF_DH/CycHdrlase_cat_dom.
IPR020631. THF_DH/CycHdrlase_NAD-bd_dom.
[Graphical view]
PfamPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802329.
PROQ8WZJ7.

Entry information

Entry nameC1TC_SCHPO
AccessionPrimary (citable) accession number: Q8WZJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways