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O43007

- C1TM_SCHPO

UniProt

O43007 - C1TM_SCHPO

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Protein
C-1-tetrahydrofolate synthase, mitochondrial
Gene
ade9, SPBC2G2.08
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 sitei227 – 2271NADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi202 – 2043NADP By similarity
Nucleotide bindingi405 – 4128ATP 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

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. purine nucleobase biosynthetic process Source: PomBase
  6. purine nucleotide biosynthetic process Source: UniProtKB-KW
  7. 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, mitochondrial
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
Name:ade9
ORF Names:SPBC2G2.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC2G2.08.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555Mitochondrion Reviewed prediction
Add
BLAST
Chaini56 – 972917C-1-tetrahydrofolate synthase, mitochondrialUniRule annotation
PRO_0000315627Add
BLAST

Proteomic databases

MaxQBiO43007.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi276831. 4 interactions.
MINTiMINT-4674578.
STRINGi4896.SPBC2G2.08-1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 340285Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseUniRule annotation
Add
BLAST
Regioni84 – 885Substrate binding By similarity
Regioni131 – 1333Substrate binding By similarity
Regioni299 – 3035Substrate binding By similarity
Regioni341 – 972632Formyltetrahydrofolate 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.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0190.
HOGENOMiHOG000040280.
KOiK00288.
OrthoDBiEOG7K0ZMJ.

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.
IPR020867. THF_DH/CycHdrlase_CS.
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.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43007-1 [UniParc]FASTAAdd to Basket

« Hide

MNVMVSFNQL RNYFLESNSL RPSKWLFQSY GTSSSANILN GKLLARKLQR    50
SVAEEVQALK AKDRNFKPAL AIVQVGKRED SNVYVRMKEK AARLVGIDFK 100
YCPFPETIQM PALLHELKKL NDDHTVHGVL VQLPLPKHLN ERTVTESITP 150
PKDVDGFGAF NIGLLAKNDA TPIHYPCTPK GIMELLKDNK ISVAGLNAVV 200
LGRSDIVGNP ISYLLRKDNA TVTVCHSKTK DLIQHISNAD LVIAALGKPE 250
FVRGEWLKPG SVVVDVGINA VQRNGKRVLV GDVHFESASK VASSITPVPG 300
GVGPMTVAML MENIVNAAKI ARTENIYRKI DLNPLELKKP VPSDIEIANS 350
QEPKLISNLA KEMGIYDTEL ENYGNYKAKV NLAVYERLKH RKDGNYVVVS 400
GITPTPFGEG KSTVVAGLVQ AMGHLGKLGI ACVRQPSQGP TFGVKGGAAG 450
GGYAQFIPMD DFNLHMTGDI HAVTAANNLL VAALETRMFH ENTQSDAALI 500
KRLIPVKNGR RVIPRGLIGR WNRICASHNM DPEDVNNASP ELLKEFVRLN 550
VDPDTIECNR VLDVNDRFLR SIEVGKASTE KGHVRKTSFD ISVASECMSI 600
LALSCDLNDM HSRLSRMVIA NDKYGNAITA GDLGVSGALT VLLKDAIKPN 650
LMQTLEGTPA FVHAGPFANI SIGASSIIAD KIALKLAGTE SFDRPEDAGY 700
VVTEAGFASD MGMEKFFNIK CRYSKLVPNT VVLVTTVKAL KLHGGGPKLK 750
PGAPIPEEYL VENLDLVKNG CSNMVKHIQN CHKFNIPVVV AINSYKTDSS 800
KEHEIIREAA LQAGAVDAVP SDHWAQGGKG AIELAKSVMT ACDQSSNSKF 850
RLLYDSETSI EDKVNVIAKE MYGANGVEFS SLAKERINTF IKQGFGNLPI 900
CMAKTQYSLS HNPEFRNVPK NFTVPIRDMR LNAGAGFIYP LAAEIQTIPG 950
LPTAPAYLNI DICENGEIVG LS 972
Length:972
Mass (Da):105,757
Last modified:October 3, 2012 - v3
Checksum:iA14DFE32C0106F20
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAA17888.3.
PIRiT40147.
RefSeqiNP_596437.2. NM_001022356.2.

Genome annotation databases

EnsemblFungiiSPBC2G2.08.1; SPBC2G2.08.1:pep; SPBC2G2.08.
GeneIDi2540300.
KEGGispo:SPBC2G2.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAA17888.3 .
PIRi T40147.
RefSeqi NP_596437.2. NM_001022356.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 276831. 4 interactions.
MINTi MINT-4674578.
STRINGi 4896.SPBC2G2.08-1.

Proteomic databases

MaxQBi O43007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC2G2.08.1 ; SPBC2G2.08.1:pep ; SPBC2G2.08 .
GeneIDi 2540300.
KEGGi spo:SPBC2G2.08.

Organism-specific databases

PomBasei SPBC2G2.08.

Phylogenomic databases

eggNOGi COG0190.
HOGENOMi HOG000040280.
KOi K00288.
OrthoDBi EOG7K0ZMJ.

Enzyme and pathway databases

UniPathwayi UPA00193 .

Miscellaneous databases

NextBioi 20801430.

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.
IPR020867. THF_DH/CycHdrlase_CS.
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.
PS00767. THF_DHG_CYH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "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 nameiC1TM_SCHPO
AccessioniPrimary (citable) accession number: O43007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2012
Last modified: June 11, 2014
This is version 86 of the entry and version 3 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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