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P09440

- C1TM_YEAST

UniProt

P09440 - C1TM_YEAST

Protein

C-1-tetrahydrofolate synthase, mitochondrial

Gene

MIS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 sitei226 – 2261NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi201 – 2033NADPBy similarity
    Nucleotide bindingi408 – 4158ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. folic acid biosynthetic process Source: SGD
    2. histidine biosynthetic process Source: UniProtKB-KW
    3. methionine biosynthetic process Source: UniProtKB-KW
    4. nucleobase-containing compound metabolic process Source: SGD
    5. purine nucleotide biosynthetic process Source: UniProtKB-KW
    6. 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

    BioCyciYEAST:YBR084W-MONOMER.
    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:MIS1
    Ordered Locus Names:YBR084W
    ORF Names:YBR0751
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR084w.
    SGDiS000000288. MIS1.

    Subcellular locationi

    Mitochondrion 3 Publications

    GO - Cellular componenti

    1. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434Mitochondrion1 PublicationAdd
    BLAST
    Chaini35 – 975941C-1-tetrahydrofolate synthase, mitochondrialPRO_0000034052Add
    BLAST

    Proteomic databases

    MaxQBiP09440.
    PaxDbiP09440.
    PeptideAtlasiP09440.
    PRIDEiP09440.

    Expressioni

    Gene expression databases

    GenevestigatoriP09440.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RPB5P204341EBI-3903,EBI-15781
    SAT4P253331EBI-3903,EBI-16492
    YHR080CP388001EBI-3903,EBI-24597

    Protein-protein interaction databases

    BioGridi32788. 95 interactions.
    DIPiDIP-6724N.
    IntActiP09440. 50 interactions.
    MINTiMINT-660665.
    STRINGi4932.YBR084W.

    Structurei

    3D structure databases

    ProteinModelPortaliP09440.
    SMRiP09440. Positions 37-326, 344-975.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 343309Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
    BLAST
    Regioni83 – 875Substrate bindingBy similarity
    Regioni130 – 1323Substrate bindingBy similarity
    Regioni301 – 3055Substrate bindingBy similarity
    Regioni344 – 975632Formyltetrahydrofolate 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.
    GeneTreeiENSGT00750000117947.
    HOGENOMiHOG000040280.
    KOiK00288.
    OMAiLPTHAGF.
    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.
    PS00722. FTHFS_2. 1 hit.
    PS00766. THF_DHG_CYH_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.

    P09440-1 [UniParc]FASTAAdd to Basket

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    MLSRLSLLSN SRAFQQARWR IYRLKVSPTV HASQYHILSG RKLAQSIREK    50
    ANDEIQAIKL KHPNFKPTLK IIQVGARPDS STYVRMKLKA SKDSNVDCII 100
    EKLPAEITEV ELLKKISDIN DDDSIHGLLI QLPLPRHLDE TTITNAVDFK 150
    KDVDGFHRYN AGELAKKGGK PYFIPCTPYG CMKLLEEAHV KLDGKNAVVL 200
    GRSSIVGNPI ASLLKNANAT VTVCHSHTRN IAEVVSQADI VIAACGIPQY 250
    VKSDWIKEGA VVIDVGINYV PDISKKSGQK LVGDVDFDSV KEKTSYITPV 300
    PGGVGPMTVA MLVSNVLLAA KRQFVESEKL PVIKPLPLHL ESPVPSDIDI 350
    SRAQSPKHIK QVAEELGIHS HELELYGHYK AKISPNIFKR LESRENGKYV 400
    LVAGITPTPL GEGKSTTTMG LVQALSAHLG KPSIANVRQP SLGPTLGVKG 450
    GAAGGGYAQV IPMDEFNLHL TGDIHAISAA NNLLAAAIDT RMFHEATQKN 500
    DSTFYKRLVP RKKGIRKFTP SMQRRLKRLD IEKEDPDALT PEEVKRFARL 550
    NINPDTITIR RVVDINDRML RQITIGEAAT EKGFTRTTGF DITVASELMA 600
    ILALSKSLHE MKERIGRMVI GADYDNKPVT VEDIGCTGAL TALLRDAIKP 650
    NLMQTLEGTP VMVHAGPFAN ISIGASSVIA DLMALKLVGS EKNPLNDKNI 700
    HEPGYVVTEA GFDFAMGGER FFDIKCRSSG LVPDAVVLVA TVRALKSHGG 750
    APNVKPGQSL PKEYTEENID FVAKGVSNLV KQIENIKTFG IPVVVAINRF 800
    ETDSQAEIEV IKKAALNAGA SHAVTSNHWM EGGKGAVELA HAVVDATKEP 850
    KNFNFLYDVN SSIEDKLTSI VQKMYGGAKI EVSPEAQKKI DTYKKQGFGN 900
    LPICIAKTQY SLSHDPSLKG VPRGFTFPIR DVRASIGAGY LYALAAEIQT 950
    IPGLSTYAGY MAVEVDDDGE IEGLF 975
    Length:975
    Mass (Da):106,217
    Last modified:July 1, 1989 - v1
    Checksum:iB9421D4F8981531F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35953 Genomic DNA. Translation: CAA85029.1.
    J03724 Genomic DNA. Translation: AAA34781.1.
    BK006936 Genomic DNA. Translation: DAA07203.1.
    PIRiA28174.
    RefSeqiNP_009640.1. NM_001178432.1.

    Genome annotation databases

    EnsemblFungiiYBR084W; YBR084W; YBR084W.
    GeneIDi852378.
    KEGGisce:YBR084W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35953 Genomic DNA. Translation: CAA85029.1 .
    J03724 Genomic DNA. Translation: AAA34781.1 .
    BK006936 Genomic DNA. Translation: DAA07203.1 .
    PIRi A28174.
    RefSeqi NP_009640.1. NM_001178432.1.

    3D structure databases

    ProteinModelPortali P09440.
    SMRi P09440. Positions 37-326, 344-975.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32788. 95 interactions.
    DIPi DIP-6724N.
    IntActi P09440. 50 interactions.
    MINTi MINT-660665.
    STRINGi 4932.YBR084W.

    Proteomic databases

    MaxQBi P09440.
    PaxDbi P09440.
    PeptideAtlasi P09440.
    PRIDEi P09440.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR084W ; YBR084W ; YBR084W .
    GeneIDi 852378.
    KEGGi sce:YBR084W.

    Organism-specific databases

    CYGDi YBR084w.
    SGDi S000000288. MIS1.

    Phylogenomic databases

    eggNOGi COG0190.
    GeneTreei ENSGT00750000117947.
    HOGENOMi HOG000040280.
    KOi K00288.
    OMAi LPTHAGF.
    OrthoDBi EOG7K0ZMJ.

    Enzyme and pathway databases

    UniPathwayi UPA00193 .
    BioCyci YEAST:YBR084W-MONOMER.

    Miscellaneous databases

    NextBioi 971174.

    Gene expression databases

    Genevestigatori P09440.

    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.
    PS00722. FTHFS_2. 1 hit.
    PS00766. THF_DHG_CYH_1. 1 hit.
    PS00767. THF_DHG_CYH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase."
      Shannon K.W., Rabinowitz J.C.
      J. Biol. Chem. 263:7717-7725(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae."
      Shannon K.W., Rabinowitz J.C.
      J. Biol. Chem. 261:12266-12271(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-74, CHARACTERIZATION, SUBCELLULAR LOCATION, SUBUNIT.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.

    Entry informationi

    Entry nameiC1TM_YEAST
    AccessioniPrimary (citable) accession number: P09440
    Secondary accession number(s): D6VQ83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 11400 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3