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O43007

- C1TM_SCHPO

UniProt

O43007 - C1TM_SCHPO

Protein

C-1-tetrahydrofolate synthase, mitochondrial

Gene

ade9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei227 – 2271NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi202 – 2043NADPBy similarity
    Nucleotide bindingi405 – 4128ATPBy 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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5555MitochondrionSequence AnalysisAdd
    BLAST
    Chaini56 – 972917C-1-tetrahydrofolate synthase, mitochondrialPRO_0000315627Add
    BLAST

    Proteomic databases

    MaxQBiO43007.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    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 cyclohydrolaseAdd
    BLAST
    Regioni84 – 885Substrate bindingBy similarity
    Regioni131 – 1333Substrate bindingBy similarity
    Regioni299 – 3035Substrate bindingBy similarity
    Regioni341 – 972632Formyltetrahydrofolate 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

    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

    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: October 1, 2014
    This is version 87 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