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O96553

- C1TC_DROME

UniProt

O96553 - C1TC_DROME

Protein

C-1-tetrahydrofolate synthase, cytoplasmic

Gene

pug

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 4 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei230 – 2301NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi205 – 2073NADPBy similarity
    Nucleotide bindingi413 – 4208ATPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: UniProtKB
    2. folic acid-containing compound biosynthetic process Source: InterPro
    3. histidine biosynthetic process Source: UniProtKB-KW
    4. methionine biosynthetic process Source: UniProtKB-KW
    5. one-carbon metabolic process Source: RefGenome
    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, 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
    Name:pug
    ORF Names:CG4067
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0020385. pug.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. lipid particle Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 968968C-1-tetrahydrofolate synthase, cytoplasmicPRO_0000199324Add
    BLAST

    Proteomic databases

    PaxDbiO96553.
    PRIDEiO96553.

    Expressioni

    Tissue specificityi

    Present in all tissues.1 Publication

    Gene expression databases

    BgeeiO96553.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Keap1Q9VEN51EBI-118733,EBI-181742

    Protein-protein interaction databases

    BioGridi66423. 2 interactions.
    IntActiO96553. 1 interaction.
    MINTiMINT-297603.

    Structurei

    3D structure databases

    ProteinModelPortaliO96553.
    SMRiO96553. Positions 38-329, 350-968.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 338338Methylenetetrahydrofolate dehydrogenase and cyclohydrolaseAdd
    BLAST
    Regioni86 – 905Substrate bindingBy similarity
    Regioni133 – 1353Substrate bindingBy similarity
    Regioni305 – 3095Substrate bindingBy similarity
    Regioni339 – 968630Formyltetrahydrofolate synthetaseAdd
    BLAST

    Domaini

    This trifunctional enzyme consists of two major domains: a N-terminal part, containing the methylene-THF dehydrogenase and the methenyl-THF cyclohydrolase activities and a larger formyl-THF synthetase domain.

    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.
    GeneTreeiENSGT00750000117401.
    InParanoidiO96553.
    KOiK00288.
    OMAiFAPLMFK.
    OrthoDBiEOG76T9QN.
    PhylomeDBiO96553.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: O96553-1) [UniParc]FASTAAdd to Basket

    Also known as: D

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSAQYQRFLK VLEKWPAEKS KVGSGEWTAE PAIKMSGAKI ISGTAVAKSI    50
    REELRNEVTA MSKQLADFVP GLRIVQVGGR EDSNVYIRMK IKAATEIGID 100
    AAHVQLPRSI TEVELLDKIN DLNEDPRVHG IIVQMPLDCD TPIDSHRITD 150
    AVSPEKDVDG LHTVNEGRLA IGDLGGFLPC TPWGCLELIR RSGVEIAGAR 200
    AVVLGRSKIV GTPAAELLKW ANATVTVCHS KTRNLEEITR SADILVVGIG 250
    VAEMVKGSWI KPGAVVIDCG INVKPDASKA SGSKLVGDVD YAEALQVAGH 300
    LTPVPGGVGP MTVAMLMKNT VRSAARFLER LAKSQWALQT LPLKPQRPVP 350
    SDIVIARAQK PKDIAVLAKE IGLEAREVSL YGNKKAKISL SVLERLKDKE 400
    VGHYVVVAGM TPTPLGEGKT TTLMGLVQAL GAHKLRNTMA ALRQPSQGPT 450
    FGIKGGAAGG GYAQVIPMEE FNLHLTGDIH AVSAANNLLA AQLDTRIFHE 500
    NTQKDKALYD RLVPAIKGQR KFSPIQLRRL QKLGITKTDP DTLTADEYGP 550
    FARLDIDPDT IMWERVVDIN DRYLRTITVG QSPTEKGISR ETRFSISVAS 600
    EIMAVLALSR SLEDMKQRLA DMVVAFDKRG KPVTADDLGV TGALAVLLKD 650
    ALEPNLMQSL EGTPVLVHAG PFANIAHGCN SIIADEVGLK LVGKNGFVCT 700
    EAGFGSDIGM EKFCNIKCRT SGRKPNAMVL VATVRAIKMH GGGAPVTPGA 750
    PLNKQYTEEN LELVQKGLPN LLQHIENGKA FGMPVVVSLN AHSADTPAEH 800
    ELVKKAALEA GAFAAVVSTH WADGGAGAVQ LADAVIKACE QGNQFRLLYD 850
    LELPLVDKMN KIATTMYGAG KVVLSPAAEE KVKRLTDAGF GNLPICMSKV 900
    SGSFTGDAKI KGAPKGFTLD VEDVYVSAGA GFVVAMCGEV TKMPGLPTRP 950
    AIYDIDLNTE TGEIEGLF 968

    Note: No experimental confirmation available.

    Length:968
    Mass (Da):103,504
    Last modified:July 19, 2004 - v4
    Checksum:iD65EC8455DD8AF2C
    GO
    Isoform A (identifier: O96553-2) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: Missing.

    Show »
    Length:934
    Mass (Da):99,627
    Checksum:i42CC88A69A4D5345
    GO

    Sequence cautioni

    The sequence AAL39291.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti879 – 8791E → K in AAX33426. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434Missing in isoform A. 1 PublicationVSP_010883Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082097 Genomic DNA. Translation: AAC78847.1.
    AE014297 Genomic DNA. Translation: AAG22140.2.
    AE014297 Genomic DNA. Translation: AAN13478.1.
    AE014297 Genomic DNA. Translation: AAN13479.1.
    AE014297 Genomic DNA. Translation: AAX52944.1.
    BT021278 mRNA. Translation: AAX33426.1.
    AY069146 mRNA. Translation: AAL39291.1. Different initiation.
    RefSeqiNP_001014614.1. NM_001014614.2. [O96553-1]
    NP_477254.1. NM_057906.4. [O96553-2]
    NP_731489.2. NM_169350.2. [O96553-1]
    NP_731490.1. NM_169351.2. [O96553-2]
    UniGeneiDm.14326.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082264; FBpp0081741; FBgn0020385. [O96553-1]
    FBtr0100144; FBpp0099494; FBgn0020385. [O96553-1]
    GeneIDi41279.
    KEGGidme:Dmel_CG4067.
    UCSCiCG4067-RA. d. melanogaster. [O96553-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082097 Genomic DNA. Translation: AAC78847.1 .
    AE014297 Genomic DNA. Translation: AAG22140.2 .
    AE014297 Genomic DNA. Translation: AAN13478.1 .
    AE014297 Genomic DNA. Translation: AAN13479.1 .
    AE014297 Genomic DNA. Translation: AAX52944.1 .
    BT021278 mRNA. Translation: AAX33426.1 .
    AY069146 mRNA. Translation: AAL39291.1 . Different initiation.
    RefSeqi NP_001014614.1. NM_001014614.2. [O96553-1 ]
    NP_477254.1. NM_057906.4. [O96553-2 ]
    NP_731489.2. NM_169350.2. [O96553-1 ]
    NP_731490.1. NM_169351.2. [O96553-2 ]
    UniGenei Dm.14326.

    3D structure databases

    ProteinModelPortali O96553.
    SMRi O96553. Positions 38-329, 350-968.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66423. 2 interactions.
    IntActi O96553. 1 interaction.
    MINTi MINT-297603.

    Proteomic databases

    PaxDbi O96553.
    PRIDEi O96553.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082264 ; FBpp0081741 ; FBgn0020385 . [O96553-1 ]
    FBtr0100144 ; FBpp0099494 ; FBgn0020385 . [O96553-1 ]
    GeneIDi 41279.
    KEGGi dme:Dmel_CG4067.
    UCSCi CG4067-RA. d. melanogaster. [O96553-1 ]

    Organism-specific databases

    CTDi 41279.
    FlyBasei FBgn0020385. pug.

    Phylogenomic databases

    eggNOGi COG0190.
    GeneTreei ENSGT00750000117401.
    InParanoidi O96553.
    KOi K00288.
    OMAi FAPLMFK.
    OrthoDBi EOG76T9QN.
    PhylomeDBi O96553.

    Enzyme and pathway databases

    UniPathwayi UPA00193 .

    Miscellaneous databases

    GenomeRNAii 41279.
    NextBioi 823064.
    PROi O96553.

    Gene expression databases

    Bgeei O96553.

    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. "Dominant defects in Drosophila eye pigmentation resulting from a euchromatin-heterochromatin fusion gene."
      Rong Y.S., Golic K.G.
      Genetics 150:1551-1566(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley1 Publication.
    3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-968.
      Strain: Berkeley1 Publication.
      Tissue: Head1 Publication.

    Entry informationi

    Entry nameiC1TC_DROME
    AccessioniPrimary (citable) accession number: O96553
    Secondary accession number(s): A4V2N7
    , A4V2N9, Q5BIE6, Q8T0P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 110 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3