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P53848

- FOL1_YEAST

UniProt

P53848 - FOL1_YEAST

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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

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
Complete GO annotation...

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. membrane Source: UniProtKB-KW
  3. mitochondrial envelope Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

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. 10 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 – 3069Combined sources
Beta strandi308 – 3103Combined sources
Helixi311 – 32414Combined sources
Beta strandi328 – 3336Combined sources
Beta strandi336 – 3394Combined sources
Beta strandi350 – 36112Combined sources
Helixi363 – 37715Combined sources
Beta strandi392 – 3998Combined sources
Beta strandi414 – 4163Combined sources
Helixi420 – 4223Combined sources
Helixi424 – 4307Combined sources
Turni431 – 4333Combined sources
Turni441 – 4433Combined sources
Helixi447 – 45610Combined sources
Helixi460 – 4623Combined sources
Beta strandi464 – 4707Combined sources
Beta strandi479 – 4879Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi505 – 5117Combined sources
Turni517 – 5259Combined sources
Helixi527 – 54216Combined sources
Beta strandi548 – 5536Combined sources
Helixi566 – 58217Combined sources
Beta strandi584 – 5863Combined sources
Helixi588 – 5903Combined sources
Beta strandi591 – 5966Combined sources
Helixi600 – 6089Combined sources
Beta strandi613 – 6164Combined sources
Turni617 – 6204Combined sources
Helixi626 – 6316Combined sources
Beta strandi636 – 6416Combined sources
Turni647 – 6493Combined sources
Helixi650 – 6523Combined sources
Turni660 – 6645Combined sources
Beta strandi665 – 6706Combined sources
Helixi675 – 6773Combined sources
Helixi681 – 6844Combined sources
Helixi686 – 70419Combined sources
Helixi709 – 7113Combined sources
Beta strandi712 – 7154Combined sources
Helixi724 – 7329Combined sources
Helixi734 – 7374Combined sources
Beta strandi740 – 7467Combined sources
Beta strandi749 – 7546Combined sources
Beta strandi760 – 7623Combined sources
Helixi768 – 7747Combined sources
Helixi779 – 7824Combined sources
Helixi783 – 79513Combined sources
Beta strandi799 – 8046Combined sources
Helixi806 – 82116Combined sources

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.
InParanoidiP53848.
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

        10         20         30         40         50
MSKLFSTVNS ARHSVPLGGM RDYVHIKKLE MNTVLGPDSW NQLMPQKCLL
60 70 80 90 100
SLDMGTDFSK SAATDDLKYS LNYAVISRDL TNFVSKKKNW GSVSNLAKSV
110 120 130 140 150
SQFVMDKYSG VECLNLEVQA DTTHIRSDHI SCIIQQERGN PESQEFDVVR
160 170 180 190 200
ISELKMLTLI GVFTFERLKK QYVTLDIKLP WPKKAELPPP VQSIIDNVVK
210 220 230 240 250
FVEESNFKTV EALVESVSAV IAHNEYFQKF PDSPLVVKVL KLNAITATEG
260 270 280 290 300
VGVSCIREPR EIAMVNIPYL SSIHESSDIK FQLSSSQNTP IEGKNTWKRA
310 320 330 340 350
FLAFGSNIGD RFKHIQMALQ LLSREKTVKL RNISSIFESE PMYFKDQTPF
360 370 380 390 400
MNGCVEVETL LTPSELLKLC KKIEYEELQR VKHFDNGPRT IDLDIVMFLN
410 420 430 440 450
SAGEDIIVNE PDLNIPHPRM LERTFVLEPL CELISPVHLH PVTAEPIVDH
460 470 480 490 500
LKQLYDKQHD EDTLWKLVPL PYRSGVEPRF LKFKTATKLD EFTGETNRIT
510 520 530 540 550
VSPTYIMAIF NATPDSFSDG GEHFADIESQ LNDIIKLCKD ALYLHESVII
560 570 580 590 600
DVGGCSTRPN SIQASEEEEI RRSIPLIKAI RESTELPQDK VILSIDTYRS
610 620 630 640 650
NVAKEAIKVG VDIINDISGG LFDSNMFAVI AENPEICYIL SHTRGDISTM
660 670 680 690 700
NRLAHYENFA LGDSIQQEFV HNTDIQQLDD LKDKTVLIRN VGQEIGERYI
710 720 730 740 750
KAIDNGVKRW QILIDPGLGF AKTWKQNLQI IRHIPILKNY SFTMNSNNSQ
760 770 780 790 800
VYVNLRNMPV LLGPSRKKFI GHITKDVDAK QRDFATGAVV ASCIGFGSDM
810 820
VRVHDVKNCS KSIKLADAIY KGLE
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. 10 interactions.
IntActi P53848. 7 interactions.
MINTi MINT-2784107.
STRINGi 4932.YNL256W.

Chemistry

DrugBanki DB00634. Sulfacetamide.

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.
InParanoidi P53848.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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