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P53848 (FOL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Folic acid synthesis protein FOL1

Including the following 3 domains:

  1. Dihydroneopterin aldolase
    Short name=DHNA
    EC=4.1.2.25
    Alternative name(s):
    FASA
    FASB
  2. 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
  3. Dihydropteroate synthase
    Short name=DHPS
    EC=2.5.1.15
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    FASD
Gene names
Name:FOL1
Ordered Locus Names:YNL256W
ORF Names:N0848
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length824 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes three sequential steps of tetrahydrofolate biosynthesis. Ref.8

Catalytic activity

2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde. Ref.8

ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate. Ref.8

(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate. Ref.8

Cofactor

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

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.

Subunit structure

Homodimer. Interacts with NAP1. Ref.9 Ref.13

Subcellular location

Mitochondrion membrane Ref.7 Ref.8.

Miscellaneous

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

Sequence similarities

In the N-terminal section; belongs to the DHNA family.

In the central section; belongs to the HPPK family.

In the C-terminal section; belongs to the DHPS family.

Contains 1 pterin-binding domain.

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 824823Folic acid synthesis protein FOL1
PRO_0000168243

Regions

Domain504 – 814311Pterin-binding
Region22 – 144123DHNA 1
Region147 – 284138DHNA 2
Region295 – 466172HPPK
Region479 – 824346DHPS
Region557 – 5582Substrate binding

Sites

Metal binding5111Magnesium By similarity
Binding site5191Substrate
Binding site5961Substrate
Binding site6151Substrate
Binding site7151Substrate
Binding site7671Substrate
Binding site8021Substrate
Binding site8041Substrate

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue2861Phosphoserine Ref.11

Secondary structure

............................................................................................. 824
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53848 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: D66986D8E2EB39E7

FASTA82493,120
        10         20         30         40         50         60 
MSKLFSTVNS ARHSVPLGGM RDYVHIKKLE MNTVLGPDSW NQLMPQKCLL SLDMGTDFSK 

        70         80         90        100        110        120 
SAATDDLKYS LNYAVISRDL TNFVSKKKNW GSVSNLAKSV SQFVMDKYSG VECLNLEVQA 

       130        140        150        160        170        180 
DTTHIRSDHI SCIIQQERGN PESQEFDVVR ISELKMLTLI GVFTFERLKK QYVTLDIKLP 

       190        200        210        220        230        240 
WPKKAELPPP VQSIIDNVVK FVEESNFKTV EALVESVSAV IAHNEYFQKF PDSPLVVKVL 

       250        260        270        280        290        300 
KLNAITATEG VGVSCIREPR EIAMVNIPYL SSIHESSDIK FQLSSSQNTP IEGKNTWKRA 

       310        320        330        340        350        360 
FLAFGSNIGD RFKHIQMALQ LLSREKTVKL RNISSIFESE PMYFKDQTPF MNGCVEVETL 

       370        380        390        400        410        420 
LTPSELLKLC KKIEYEELQR VKHFDNGPRT IDLDIVMFLN SAGEDIIVNE PDLNIPHPRM 

       430        440        450        460        470        480 
LERTFVLEPL CELISPVHLH PVTAEPIVDH LKQLYDKQHD EDTLWKLVPL PYRSGVEPRF 

       490        500        510        520        530        540 
LKFKTATKLD EFTGETNRIT VSPTYIMAIF NATPDSFSDG GEHFADIESQ LNDIIKLCKD 

       550        560        570        580        590        600 
ALYLHESVII DVGGCSTRPN SIQASEEEEI RRSIPLIKAI RESTELPQDK VILSIDTYRS 

       610        620        630        640        650        660 
NVAKEAIKVG VDIINDISGG LFDSNMFAVI AENPEICYIL SHTRGDISTM NRLAHYENFA 

       670        680        690        700        710        720 
LGDSIQQEFV HNTDIQQLDD LKDKTVLIRN VGQEIGERYI KAIDNGVKRW QILIDPGLGF 

       730        740        750        760        770        780 
AKTWKQNLQI IRHIPILKNY SFTMNSNNSQ VYVNLRNMPV LLGPSRKKFI GHITKDVDAK 

       790        800        810        820 
QRDFATGAVV ASCIGFGSDM VRVHDVKNCS KSIKLADAIY KGLE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS63229.
RefSeqNP_014143.2. NM_001183094.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BMBX-ray2.30A297-824[»]
ProteinModelPortalP53848.
SMRP53848. Positions 22-138, 146-824.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35583. 9 interactions.
IntActP53848. 7 interactions.
MINTMINT-2784107.
STRING4932.YNL256W.

Proteomic databases

PaxDbP53848.
PeptideAtlasP53848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL256W; YNL256W; YNL256W.
GeneID855465.
KEGGsce:YNL256W.

Organism-specific databases

CYGDYNL256w.
SGDS000005200. FOL1.

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217511.
KOK13939.
OMAFRNGPRA.
OrthoDBEOG7RZ5ZF.

Enzyme and pathway databases

BioCycYEAST:YNL256W-MONOMER.
BRENDA2.5.1.15. 984.
UniPathwayUPA00077; UER00154.
UPA00077; UER00155.
UPA00077; UER00156.

Gene expression databases

GenevestigatorP53848.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
3.30.70.560. 1 hit.
InterProIPR011005. Dihydropteroate_synth-like.
IPR006157. FolB_dom.
IPR016261. Folic_acid_synth.
IPR000550. Hppk.
IPR000489. Pterin-binding.
[Graphical view]
PfamPF02152. FolB. 2 hits.
PF01288. HPPK. 1 hit.
PF00809. Pterin_bind. 1 hit.
[Graphical view]
PIRSFPIRSF000741. Folic_acid_synth. 1 hit.
SMARTSM00905. FolB. 2 hits.
[Graphical view]
SUPFAMSSF51717. SSF51717. 2 hits.
SSF55083. SSF55083. 1 hit.
TIGRFAMsTIGR00526. folB_dom. 2 hits.
TIGR01498. folK. 1 hit.
PROSITEPS00792. DHPS_1. 1 hit.
PS00793. DHPS_2. 1 hit.
PS00794. HPPK. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP53848.
NextBio979400.

Entry information

Entry nameFOL1_YEAST
AccessionPrimary (citable) accession number: P53848
Secondary accession number(s): D6W0T7, Q2VQX0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways