Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene

SPBC839.16

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH.
5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate.
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate.

Pathway: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei193 – 1931NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 1703NADPBy similarity
Nucleotide bindingi374 – 3818ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • formate-tetrahydrofolate ligase activity Source: PomBase
  • methenyltetrahydrofolate cyclohydrolase activity Source: PomBase
  • methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: PomBase
  • single-stranded DNA binding Source: PomBase

GO - Biological processi

  • 10-formyltetrahydrofolate biosynthetic process Source: PomBase
  • folic acid biosynthetic process Source: PomBase
  • histidine biosynthetic process Source: UniProtKB-KW
  • methionine biosynthetic process Source: UniProtKB-KW
  • one-carbon metabolic process Source: PomBase
  • purine nucleobase biosynthetic process Source: PomBase
  • purine nucleotide biosynthetic process Source: UniProtKB-KW
  • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Methionine biosynthesis, One-carbon metabolism, Purine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_333030. Metabolism of folate and pterines.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
C-1-tetrahydrofolate synthase, cytoplasmic
Short name:
C1-THF synthase
Including the following 3 domains:
Methylenetetrahydrofolate dehydrogenase (EC:1.5.1.5)
Methenyltetrahydrofolate cyclohydrolase (EC:3.5.4.9)
Formyltetrahydrofolate synthetase (EC:6.3.4.3)
Gene namesi
ORF Names:SPBC839.16
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC839.16.
PomBaseiSPBC839.16.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 937937C-1-tetrahydrofolate synthase, cytoplasmicPRO_0000315626Add
BLAST

Proteomic databases

MaxQBiQ8WZJ7.
PaxDbiQ8WZJ7.
PRIDEiQ8WZJ7.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-4700994.
STRINGi4896.SPBC839.16.1.

Structurei

3D structure databases

ProteinModelPortaliQ8WZJ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 309309Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
BLAST
Regioni50 – 545Substrate bindingBy similarity
Regioni97 – 993Substrate bindingBy similarity
Regioni268 – 2725Substrate bindingBy similarity
Regioni310 – 937628Formyltetrahydrofolate synthetaseAdd
BLAST

Domaini

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 similaritiesi

In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.Curated
In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family.Curated

Phylogenomic databases

eggNOGiCOG0190.
HOGENOMiHOG000040280.
InParanoidiQ8WZJ7.
KOiK00288.
OMAiFAPLMFK.
OrthoDBiEOG7K0ZMJ.
PhylomeDBiQ8WZJ7.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. 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]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8WZJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLLEGTSL ARKVREELRE QISSIKSVDP YFNVSLKIIQ VGGREDSNVY
60 70 80 90 100
VRMKTRAANE AGISCEHVNF PEDITEYDLL LAIKGFNEDP TVHGIIVQLP
110 120 130 140 150
LPAHINEQII TEAVAPEKDV DGFCETNLGK LTKREGQPLF TACTPKGIMC
160 170 180 190 200
ILKHYGINVQ GKHAVVIGRS NIVGRPMSIL LEKANATVTL CHSKTESIAD
210 220 230 240 250
IVRTADIVVA AIGIPHFVKA DWLKKGVVAI DVGINSIPDA TKKSGYRLTG
260 270 280 290 300
DIDFENAKEV ASAITPVPGS VGPMTVAMLL QNVVESAVRF RKMSRKRKPT
310 320 330 340 350
LLPLKLQTPV PSDIEIARSQ TPKNIGDLAS EIGIAKSELE FYGSHKAKVN
360 370 380 390 400
LEILQRLAHR RDGHYVVVTG ITPTPFGEGK STLTAGLVQA LSNLDKLAIA
410 420 430 440 450
CVRQPSQGPT FGIKGGAAGG GYSQFIPMEE FNLHLTGDIH AITAATNLLA
460 470 480 490 500
AAIDTRMFHE NTQSDAALYK RLTLVKGNKR EFAPVMFRRL KKLGIDKTNP
510 520 530 540 550
EELTEEEQRK FARLDIEPST ISWNRTLDVN DRFLRKITIG ENPTEKGFTR
560 570 580 590 600
QTGFDLSVAS ECMSVLALAT DLKDMRERLG RMVVASNKSG EPVTADDLGV
610 620 630 640 650
GGALTVLLKD AIKPTLMQTL EGTPALVHAG PFANISIGAS SILADRIALK
660 670 680 690 700
LAGTEVDEDA KKEAGYVVTE AGFASDIGME KFFNIKCRTS GLKPDAIVIV
710 720 730 740 750
ATVQALKLHG GGPPVGPGKP IPEVYKREDV DLVRKGCANL AKHISNARKY
760 770 780 790 800
GLPVVVAINK FSSDSPNEIS AIREEALAAG ATDAVDSNHW AEGGKGALGV
810 820 830 840 850
ARALINACEN VDSEFRLLYD VHEPIEKKIE IIAKEMYGAD GIELSPLAKE
860 870 880 890 900
RLETFTKQGY NNLPICIAKT QYSLSHDPDL KGAPTNFTVP IRDMRLSAGA
910 920 930
GFIYPLAAAI STIPGLPTKP AYYNIDIAEN GDIVGLS
Length:937
Mass (Da):101,203
Last modified:March 1, 2002 - v1
Checksum:i70FF8700FD023C90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB46709.1.
PIRiT40723.
RefSeqiNP_595256.1. NM_001021162.2.

Genome annotation databases

EnsemblFungiiSPBC839.16.1; SPBC839.16.1:pep; SPBC839.16.
GeneIDi2541217.
KEGGispo:SPBC839.16.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB46709.1.
PIRiT40723.
RefSeqiNP_595256.1. NM_001021162.2.

3D structure databases

ProteinModelPortaliQ8WZJ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4700994.
STRINGi4896.SPBC839.16.1.

Proteomic databases

MaxQBiQ8WZJ7.
PaxDbiQ8WZJ7.
PRIDEiQ8WZJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC839.16.1; SPBC839.16.1:pep; SPBC839.16.
GeneIDi2541217.
KEGGispo:SPBC839.16.

Organism-specific databases

EuPathDBiFungiDB:SPBC839.16.
PomBaseiSPBC839.16.

Phylogenomic databases

eggNOGiCOG0190.
HOGENOMiHOG000040280.
InParanoidiQ8WZJ7.
KOiK00288.
OMAiFAPLMFK.
OrthoDBiEOG7K0ZMJ.
PhylomeDBiQ8WZJ7.

Enzyme and pathway databases

UniPathwayiUPA00193.
ReactomeiREACT_333030. Metabolism of folate and pterines.

Miscellaneous databases

NextBioi20802329.
PROiQ8WZJ7.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPiMF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProiIPR000559. 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]
PfamiPF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view]
PRINTSiPR00085. THFDHDRGNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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].

Entry informationi

Entry nameiC1TC_SCHPO
AccessioniPrimary (citable) accession number: Q8WZJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.