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Reviewed, UniProtKB/Swiss-Prot Q8WZJ7 (C1TC_SCHPO)

Last modified November 25, 2008. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    C-1-tetrahydrofolate synthase, cytoplasmic
      Short name=C1-THF synthase
Including the following 3 domains:
    1- Recommended name:
            Methylenetetrahydrofolate dehydrogenase
              EC=1.5.1.5
    2- Recommended name:
            Methenyltetrahydrofolate cyclohydrolase
              EC=3.5.4.9
    3- Recommended name:
            Formyltetrahydrofolate synthetase
              EC=6.3.4.3
Gene names
ORF Names: SPBC839.16
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH.

5,10-methenyltetrahydrofolate + H(2)O = 10-formyltetrahydrofolate.

ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Pathway

One-carbon metabolism; tetrahydrofolate pathway.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 937937C-1-tetrahydrofolate synthase, cytoplasmic
PRO_0000315626

Regions

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

Sites

Binding site1931NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WZJ7-1 [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 

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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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[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: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAB46709.1.
PIRT40723.
RefSeqNP_595256.1.

3D structure databases

HSSPHSSP built from PDB template 1A4I based on UniProtKB P11586.
ModBaseSearch...

Genome annotation databases

GeneID2541217.
KEGGspo:SPBC839.16.
NMPDRfig|4896.1.peg.1122.

Organism-specific databases

GeneDB_SpombeSPBC839.16.

Gene expression databases

ArrayExpressQ8WZJ7.

Family and domain databases

InterProIPR000559. Fmtethyd_synth.
IPR016040. NAD(P)-bd.
IPR000672. THF_DHase/CycOHase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSPR00085. THFDHDRGNASE.
ProDomPD002300. THFDhg/Cyc_hydro. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: November 25, 2008
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents