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P53848

- FOL1_YEAST

UniProt

P53848 - FOL1_YEAST

Protein

Folic acid synthesis protein FOL1

Gene

FOL1

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 138 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Catalyzes three sequential steps of tetrahydrofolate biosynthesis.1 Publication

    Catalytic activityi

    2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.1 Publication
    ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.1 Publication
    (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

    Cofactori

    Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi511 – 5111MagnesiumBy similarity
    Binding sitei519 – 5191Substrate
    Binding sitei596 – 5961Substrate
    Binding sitei615 – 6151Substrate
    Binding sitei715 – 7151Substrate
    Binding sitei767 – 7671Substrate
    Binding sitei802 – 8021Substrate
    Binding sitei804 – 8041Substrate

    GO - Molecular functioni

    1. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. dihydroneopterin aldolase activity Source: SGD
    4. dihydropteroate synthase activity Source: SGD
    5. kinase activity Source: UniProtKB-KW
    6. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. folic acid biosynthetic process Source: UniProtKB-KW
    2. tetrahydrofolate biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Kinase, Lyase, Transferase

    Keywords - Biological processi

    Folate biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:YNL256W-MONOMER.
    BRENDAi2.5.1.15. 984.
    UniPathwayiUPA00077; UER00154.
    UPA00077; UER00155.
    UPA00077; UER00156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Folic acid synthesis protein FOL1
    Including the following 3 domains:
    Dihydroneopterin aldolase (EC:4.1.2.25)
    Short name:
    DHNA
    Alternative name(s):
    FASA
    FASB
    2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC:2.7.6.3)
    Alternative name(s):
    6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
    Short name:
    PPPK
    7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
    Short name:
    HPPK
    FASC
    Dihydropteroate synthase (EC:2.5.1.15)
    Short name:
    DHPS
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    FASD
    Gene namesi
    Name:FOL1
    Ordered Locus Names:YNL256W
    ORF Names:N0848
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL256w.
    SGDiS000005200. FOL1.

    Subcellular locationi

    Mitochondrion membrane 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. mitochondrial envelope Source: SGD
    3. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 824823Folic acid synthesis protein FOL1PRO_0000168243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei286 – 2861Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP53848.
    PaxDbiP53848.
    PeptideAtlasiP53848.

    Expressioni

    Gene expression databases

    GenevestigatoriP53848.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with NAP1.2 Publications

    Protein-protein interaction databases

    BioGridi35583. 9 interactions.
    IntActiP53848. 7 interactions.
    MINTiMINT-2784107.
    STRINGi4932.YNL256W.

    Structurei

    Secondary structure

    1
    824
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi298 – 3069
    Beta strandi308 – 3103
    Helixi311 – 32414
    Beta strandi328 – 3336
    Beta strandi336 – 3394
    Beta strandi350 – 36112
    Helixi363 – 37715
    Beta strandi392 – 3998
    Beta strandi414 – 4163
    Helixi420 – 4223
    Helixi424 – 4307
    Turni431 – 4333
    Turni441 – 4433
    Helixi447 – 45610
    Helixi460 – 4623
    Beta strandi464 – 4707
    Beta strandi479 – 4879
    Beta strandi498 – 5003
    Beta strandi505 – 5117
    Turni517 – 5259
    Helixi527 – 54216
    Beta strandi548 – 5536
    Helixi566 – 58217
    Beta strandi584 – 5863
    Helixi588 – 5903
    Beta strandi591 – 5966
    Helixi600 – 6089
    Beta strandi613 – 6164
    Turni617 – 6204
    Helixi626 – 6316
    Beta strandi636 – 6416
    Turni647 – 6493
    Helixi650 – 6523
    Turni660 – 6645
    Beta strandi665 – 6706
    Helixi675 – 6773
    Helixi681 – 6844
    Helixi686 – 70419
    Helixi709 – 7113
    Beta strandi712 – 7154
    Helixi724 – 7329
    Helixi734 – 7374
    Beta strandi740 – 7467
    Beta strandi749 – 7546
    Beta strandi760 – 7623
    Helixi768 – 7747
    Helixi779 – 7824
    Helixi783 – 79513
    Beta strandi799 – 8046
    Helixi806 – 82116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BMBX-ray2.30A297-824[»]
    ProteinModelPortaliP53848.
    SMRiP53848. Positions 22-138, 296-824.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53848.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini504 – 814311Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 144123DHNA 1Add
    BLAST
    Regioni147 – 284138DHNA 2Add
    BLAST
    Regioni295 – 466172HPPKAdd
    BLAST
    Regioni479 – 824346DHPSAdd
    BLAST
    Regioni557 – 5582Substrate binding

    Sequence similaritiesi

    In the N-terminal section; belongs to the DHNA family.Curated
    In the central section; belongs to the HPPK family.Curated
    In the C-terminal section; belongs to the DHPS family.Curated
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0294.
    HOGENOMiHOG000217511.
    KOiK13939.
    OMAiFRNGPRA.
    OrthoDBiEOG7RZ5ZF.

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    3.30.70.560. 1 hit.
    InterProiIPR011005. Dihydropteroate_synth-like.
    IPR006157. FolB_dom.
    IPR016261. Folic_acid_synth.
    IPR000550. Hppk.
    IPR000489. Pterin-binding.
    [Graphical view]
    PfamiPF02152. FolB. 2 hits.
    PF01288. HPPK. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000741. Folic_acid_synth. 1 hit.
    SMARTiSM00905. FolB. 2 hits.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 2 hits.
    SSF55083. SSF55083. 1 hit.
    TIGRFAMsiTIGR00526. folB_dom. 2 hits.
    TIGR01498. folK. 1 hit.
    PROSITEiPS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS00794. HPPK. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P53848-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKLFSTVNS ARHSVPLGGM RDYVHIKKLE MNTVLGPDSW NQLMPQKCLL    50
    SLDMGTDFSK SAATDDLKYS LNYAVISRDL TNFVSKKKNW GSVSNLAKSV 100
    SQFVMDKYSG VECLNLEVQA DTTHIRSDHI SCIIQQERGN PESQEFDVVR 150
    ISELKMLTLI GVFTFERLKK QYVTLDIKLP WPKKAELPPP VQSIIDNVVK 200
    FVEESNFKTV EALVESVSAV IAHNEYFQKF PDSPLVVKVL KLNAITATEG 250
    VGVSCIREPR EIAMVNIPYL SSIHESSDIK FQLSSSQNTP IEGKNTWKRA 300
    FLAFGSNIGD RFKHIQMALQ LLSREKTVKL RNISSIFESE PMYFKDQTPF 350
    MNGCVEVETL LTPSELLKLC KKIEYEELQR VKHFDNGPRT IDLDIVMFLN 400
    SAGEDIIVNE PDLNIPHPRM LERTFVLEPL CELISPVHLH PVTAEPIVDH 450
    LKQLYDKQHD EDTLWKLVPL PYRSGVEPRF LKFKTATKLD EFTGETNRIT 500
    VSPTYIMAIF NATPDSFSDG GEHFADIESQ LNDIIKLCKD ALYLHESVII 550
    DVGGCSTRPN SIQASEEEEI RRSIPLIKAI RESTELPQDK VILSIDTYRS 600
    NVAKEAIKVG VDIINDISGG LFDSNMFAVI AENPEICYIL SHTRGDISTM 650
    NRLAHYENFA LGDSIQQEFV HNTDIQQLDD LKDKTVLIRN VGQEIGERYI 700
    KAIDNGVKRW QILIDPGLGF AKTWKQNLQI IRHIPILKNY SFTMNSNNSQ 750
    VYVNLRNMPV LLGPSRKKFI GHITKDVDAK QRDFATGAVV ASCIGFGSDM 800
    VRVHDVKNCS KSIKLADAIY KGLE 824
    Length:824
    Mass (Da):93,120
    Last modified:August 30, 2005 - v2
    Checksum:iD66986D8E2EB39E7
    GO

    Sequence cautioni

    The sequence CAA65488.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA96163.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96722 Genomic DNA. Translation: CAA65488.1. Different initiation.
    Z71532 Genomic DNA. Translation: CAA96163.1. Different initiation.
    AY899248 mRNA. Translation: AAX83933.1.
    BK006947 Genomic DNA. Translation: DAA10303.1.
    PIRiS63229.
    RefSeqiNP_014143.2. NM_001183094.1.

    Genome annotation databases

    EnsemblFungiiYNL256W; YNL256W; YNL256W.
    GeneIDi855465.
    KEGGisce:YNL256W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96722 Genomic DNA. Translation: CAA65488.1 . Different initiation.
    Z71532 Genomic DNA. Translation: CAA96163.1 . Different initiation.
    AY899248 mRNA. Translation: AAX83933.1 .
    BK006947 Genomic DNA. Translation: DAA10303.1 .
    PIRi S63229.
    RefSeqi NP_014143.2. NM_001183094.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BMB X-ray 2.30 A 297-824 [» ]
    ProteinModelPortali P53848.
    SMRi P53848. Positions 22-138, 296-824.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35583. 9 interactions.
    IntActi P53848. 7 interactions.
    MINTi MINT-2784107.
    STRINGi 4932.YNL256W.

    Proteomic databases

    MaxQBi P53848.
    PaxDbi P53848.
    PeptideAtlasi P53848.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL256W ; YNL256W ; YNL256W .
    GeneIDi 855465.
    KEGGi sce:YNL256W.

    Organism-specific databases

    CYGDi YNL256w.
    SGDi S000005200. FOL1.

    Phylogenomic databases

    eggNOGi COG0294.
    HOGENOMi HOG000217511.
    KOi K13939.
    OMAi FRNGPRA.
    OrthoDBi EOG7RZ5ZF.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00154 .
    UPA00077 ; UER00155 .
    UPA00077 ; UER00156 .
    BioCyci YEAST:YNL256W-MONOMER.
    BRENDAi 2.5.1.15. 984.

    Miscellaneous databases

    EvolutionaryTracei P53848.
    NextBioi 979400.

    Gene expression databases

    Genevestigatori P53848.

    Family and domain databases

    Gene3Di 3.20.20.20. 1 hit.
    3.30.70.560. 1 hit.
    InterProi IPR011005. Dihydropteroate_synth-like.
    IPR006157. FolB_dom.
    IPR016261. Folic_acid_synth.
    IPR000550. Hppk.
    IPR000489. Pterin-binding.
    [Graphical view ]
    Pfami PF02152. FolB. 2 hits.
    PF01288. HPPK. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000741. Folic_acid_synth. 1 hit.
    SMARTi SM00905. FolB. 2 hits.
    [Graphical view ]
    SUPFAMi SSF51717. SSF51717. 2 hits.
    SSF55083. SSF55083. 1 hit.
    TIGRFAMsi TIGR00526. folB_dom. 2 hits.
    TIGR01498. folK. 1 hit.
    PROSITEi PS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS00794. HPPK. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the left arm of chromosome XIV from Saccharomyces cerevisiae."
      Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.
      Yeast 13:849-860(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [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. "Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE."
      Zhang Z., Dietrich F.S.
      Nucleic Acids Res. 33:2838-2851(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-85.
      Strain: ATCC 208353 / W303-1A.
    5. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
      Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
      Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    8. "Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth."
      Gueldener U., Koehler G.J., Haussmann C., Bacher A., Kricke J., Becher D., Hegemann J.H.
      Mol. Biol. Cell 15:3811-3828(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    9. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
      Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
      Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces cerevisiae."
      Lawrence M.C., Iliades P., Fernley R.T., Berglez J., Pilling P.A., Macreadie I.G.
      J. Mol. Biol. 348:655-670(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 297-824 IN COMPLEX WITH PTERIN-6-YL-METHYL-MONOPHOSPHATE, SUBUNIT.

    Entry informationi

    Entry nameiFOL1_YEAST
    AccessioniPrimary (citable) accession number: P53848
    Secondary accession number(s): D6W0T7, Q2VQX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4589 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3