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Q8WZJ7

- C1TC_SCHPO

UniProt

Q8WZJ7 - C1TC_SCHPO

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Protein
C-1-tetrahydrofolate synthase, cytoplasmic
Gene
SPBC839.16
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 1703NADP By similarity
Nucleotide bindingi374 – 3818ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. formate-tetrahydrofolate ligase activity Source: PomBase
  3. methenyltetrahydrofolate cyclohydrolase activity Source: PomBase
  4. methylenetetrahydrofolate dehydrogenase (NADP+) activity Source: PomBase
  5. single-stranded DNA binding Source: PomBase

GO - Biological processi

  1. 10-formyltetrahydrofolate biosynthetic process Source: PomBase
  2. folic acid biosynthetic process Source: PomBase
  3. histidine biosynthetic process Source: UniProtKB-KW
  4. methionine biosynthetic process Source: UniProtKB-KW
  5. one-carbon metabolic process Source: PomBase
  6. purine nucleobase biosynthetic process Source: PomBase
  7. purine nucleotide biosynthetic process Source: UniProtKB-KW
  8. 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

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: Chromosome II

Organism-specific databases

PomBaseiSPBC839.16.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. 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, cytoplasmicUniRule annotation
PRO_0000315626Add
BLAST

Proteomic databases

MaxQBiQ8WZJ7.
PaxDbiQ8WZJ7.
PRIDEiQ8WZJ7.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi277731. 2 interactions.
MINTiMINT-4700994.
STRINGi4896.SPBC839.16-1.

Structurei

3D structure databases

ProteinModelPortaliQ8WZJ7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 309309Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseUniRule annotation
Add
BLAST
Regioni50 – 545Substrate binding By similarity
Regioni97 – 993Substrate binding By similarity
Regioni268 – 2725Substrate binding By similarity
Regioni310 – 937628Formyltetrahydrofolate synthetaseUniRule annotation
Add
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.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0190.
HOGENOMiHOG000040280.
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

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MALLLEGTSL ARKVREELRE QISSIKSVDP YFNVSLKIIQ VGGREDSNVY    50
VRMKTRAANE AGISCEHVNF PEDITEYDLL LAIKGFNEDP TVHGIIVQLP 100
LPAHINEQII TEAVAPEKDV DGFCETNLGK LTKREGQPLF TACTPKGIMC 150
ILKHYGINVQ GKHAVVIGRS NIVGRPMSIL LEKANATVTL CHSKTESIAD 200
IVRTADIVVA AIGIPHFVKA DWLKKGVVAI DVGINSIPDA TKKSGYRLTG 250
DIDFENAKEV ASAITPVPGS VGPMTVAMLL QNVVESAVRF RKMSRKRKPT 300
LLPLKLQTPV PSDIEIARSQ TPKNIGDLAS EIGIAKSELE FYGSHKAKVN 350
LEILQRLAHR RDGHYVVVTG ITPTPFGEGK STLTAGLVQA LSNLDKLAIA 400
CVRQPSQGPT FGIKGGAAGG GYSQFIPMEE FNLHLTGDIH AITAATNLLA 450
AAIDTRMFHE NTQSDAALYK RLTLVKGNKR EFAPVMFRRL KKLGIDKTNP 500
EELTEEEQRK FARLDIEPST ISWNRTLDVN DRFLRKITIG ENPTEKGFTR 550
QTGFDLSVAS ECMSVLALAT DLKDMRERLG RMVVASNKSG EPVTADDLGV 600
GGALTVLLKD AIKPTLMQTL EGTPALVHAG PFANISIGAS SILADRIALK 650
LAGTEVDEDA KKEAGYVVTE AGFASDIGME KFFNIKCRTS GLKPDAIVIV 700
ATVQALKLHG GGPPVGPGKP IPEVYKREDV DLVRKGCANL AKHISNARKY 750
GLPVVVAINK FSSDSPNEIS AIREEALAAG ATDAVDSNHW AEGGKGALGV 800
ARALINACEN VDSEFRLLYD VHEPIEKKIE IIAKEMYGAD GIELSPLAKE 850
RLETFTKQGY NNLPICIAKT QYSLSHDPDL KGAPTNFTVP IRDMRLSAGA 900
GFIYPLAAAI STIPGLPTKP AYYNIDIAEN GDIVGLS 937
Length:937
Mass (Da):101,203
Last modified:March 1, 2002 - v1
Checksum:i70FF8700FD023C90
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB46709.1 .
PIRi T40723.
RefSeqi NP_595256.1. NM_001021162.2.

3D structure databases

ProteinModelPortali Q8WZJ7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 277731. 2 interactions.
MINTi MINT-4700994.
STRINGi 4896.SPBC839.16-1.

Proteomic databases

MaxQBi Q8WZJ7.
PaxDbi Q8WZJ7.
PRIDEi Q8WZJ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC839.16.1 ; SPBC839.16.1:pep ; SPBC839.16 .
GeneIDi 2541217.
KEGGi spo:SPBC839.16.

Organism-specific databases

PomBasei SPBC839.16.

Phylogenomic databases

eggNOGi COG0190.
HOGENOMi HOG000040280.
KOi K00288.
OMAi FAPLMFK.
OrthoDBi EOG7K0ZMJ.
PhylomeDBi Q8WZJ7.

Enzyme and pathway databases

UniPathwayi UPA00193 .

Miscellaneous databases

NextBioi 20802329.
PROi Q8WZJ7.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.40.50.720. 1 hit.
HAMAPi MF_01543. FTHFS.
MF_01576. THF_DHG_CYH.
InterProi IPR000559. 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 ]
Pfami PF01268. FTHFS. 1 hit.
PF00763. THF_DHG_CYH. 1 hit.
PF02882. THF_DHG_CYH_C. 1 hit.
[Graphical view ]
PRINTSi PR00085. THFDHDRGNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi PS00721. FTHFS_1. 1 hit.
PS00722. FTHFS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 77 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

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