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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes three sequential steps of tetrahydrofolate biosynthesis.1 Publication

Catalytic activityi

7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.1 Publication
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate.1 Publication
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.1 Publication

Cofactori

Mg2+By similarity

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 3 and 4 of the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Folic acid synthesis protein FOL1 (FOL1)
  4. Folic acid synthesis protein FOL1 (FOL1)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Folic acid synthesis protein FOL1 (FOL1)
  2. no protein annotated in this organism
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi511MagnesiumBy similarity1
Binding sitei5586-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
Binding sitei5966-hydroxymethyl-7,8-dihydropterin diphosphate1 Publication1
Binding sitei6156-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
Binding sitei7156-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1
Binding sitei7676-hydroxymethyl-7,8-dihydropterin diphosphateCombined sources1 Publication1

GO - Molecular functioni

  • 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Source: SGD
  • 7,8-dihydromonapterin aldolase activity Source: UniProtKB-EC
  • ATP binding Source: UniProtKB-KW
  • dihydroneopterin aldolase activity Source: SGD
  • dihydropteroate synthase activity Source: SGD
  • kinase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • folic acid biosynthetic process Source: UniProtKB-KW
  • 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.
2.7.6.3. 984.
UniPathwayiUPA00077; UER00154.
UPA00077; UER00155.
UPA00077; UER00156.

Names & Taxonomyi

Protein namesi
Recommended name:
Folic acid synthesis protein FOL1
Including the following 3 domains:
Dihydroneopterin aldolase1 Publication (EC:4.1.2.251 Publication)
Short name:
DHNA1 Publication
Alternative name(s):
7,8-dihydroneopterin aldolase
FASA
FASB
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (EC:2.7.6.31 Publication)
Short name:
HPPK1 Publication
Alternative name(s):
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase1 Publication
Short name:
PPPK
FASC
Dihydropteroate synthase1 Publication (EC:2.5.1.151 Publication)
Short name:
DHPS1 Publication
Alternative name(s):
Dihydropteroate pyrophosphorylase
FASD
Gene namesi
Name:FOL11 Publication
Ordered Locus Names:YNL256W
ORF Names:N0848
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL256W.
SGDiS000005200. FOL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mitochondrial envelope Source: SGD
  • mitochondrial membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Chemistry databases

DrugBankiDB00634. Sulfacetamide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001682432 – 824Folic acid synthesis protein FOL1Add BLAST823

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei286PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53848.
PRIDEiP53848.

PTM databases

iPTMnetiP53848.

Interactioni

Subunit structurei

Homodimer. Interacts with NAP1.2 Publications

Protein-protein interaction databases

BioGridi35583. 10 interactors.
IntActiP53848. 7 interactors.
MINTiMINT-2784107.

Structurei

Secondary structure

1824
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi298 – 306Combined sources9
Beta strandi308 – 310Combined sources3
Helixi311 – 324Combined sources14
Beta strandi328 – 333Combined sources6
Beta strandi336 – 339Combined sources4
Beta strandi350 – 361Combined sources12
Helixi363 – 377Combined sources15
Beta strandi392 – 399Combined sources8
Beta strandi414 – 416Combined sources3
Helixi420 – 422Combined sources3
Helixi424 – 430Combined sources7
Turni431 – 433Combined sources3
Turni441 – 443Combined sources3
Helixi447 – 456Combined sources10
Helixi460 – 462Combined sources3
Beta strandi464 – 470Combined sources7
Beta strandi479 – 487Combined sources9
Beta strandi498 – 500Combined sources3
Beta strandi505 – 511Combined sources7
Turni517 – 525Combined sources9
Helixi527 – 542Combined sources16
Beta strandi548 – 553Combined sources6
Helixi566 – 582Combined sources17
Beta strandi584 – 586Combined sources3
Helixi588 – 590Combined sources3
Beta strandi591 – 596Combined sources6
Helixi600 – 608Combined sources9
Beta strandi613 – 616Combined sources4
Turni617 – 620Combined sources4
Helixi626 – 631Combined sources6
Beta strandi636 – 641Combined sources6
Turni647 – 649Combined sources3
Helixi650 – 652Combined sources3
Turni660 – 664Combined sources5
Beta strandi665 – 670Combined sources6
Helixi675 – 677Combined sources3
Helixi681 – 684Combined sources4
Helixi686 – 704Combined sources19
Helixi709 – 711Combined sources3
Beta strandi712 – 715Combined sources4
Helixi724 – 732Combined sources9
Helixi734 – 737Combined sources4
Beta strandi740 – 746Combined sources7
Beta strandi749 – 754Combined sources6
Beta strandi760 – 762Combined sources3
Helixi768 – 774Combined sources7
Helixi779 – 782Combined sources4
Helixi783 – 795Combined sources13
Beta strandi799 – 804Combined sources6
Helixi806 – 821Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BMBX-ray2.30A297-824[»]
ProteinModelPortaliP53848.
SMRiP53848.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53848.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini504 – 814Pterin-bindingPROSITE-ProRule annotationAdd BLAST311

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 144DHNA 1Add BLAST123
Regioni147 – 284DHNA 2Add BLAST138
Regioni295 – 466HPPKAdd BLAST172
Regioni506 – 824DHPSAdd BLAST319
Regioni802 – 8046-hydroxymethyl-7,8-dihydropterin diphosphate bindingCombined sources1 Publication3

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

HOGENOMiHOG000217511.
InParanoidiP53848.
KOiK13939.
OMAiGVFTFER.
OrthoDBiEOG092C20NY.

Family and domain databases

CDDicd00534. DHNA_DHNTPE. 2 hits.
cd00739. DHPS. 1 hit.
cd00483. HPPK. 1 hit.
Gene3Di3.20.20.20. 1 hit.
3.30.70.560. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR006157. FolB_dom.
IPR016261. Folic_acid_synth.
IPR000550. Hppk.
IPR000489. Pterin-binding_dom.
[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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA96163 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BMBX-ray2.30A297-824[»]
ProteinModelPortaliP53848.
SMRiP53848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35583. 10 interactors.
IntActiP53848. 7 interactors.
MINTiMINT-2784107.

Chemistry databases

DrugBankiDB00634. Sulfacetamide.

PTM databases

iPTMnetiP53848.

Proteomic databases

MaxQBiP53848.
PRIDEiP53848.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YNL256W.
SGDiS000005200. FOL1.

Phylogenomic databases

HOGENOMiHOG000217511.
InParanoidiP53848.
KOiK13939.
OMAiGVFTFER.
OrthoDBiEOG092C20NY.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00154.
UPA00077; UER00155.
UPA00077; UER00156.
BioCyciYEAST:YNL256W-MONOMER.
BRENDAi2.5.1.15. 984.
2.7.6.3. 984.

Miscellaneous databases

EvolutionaryTraceiP53848.
PROiP53848.

Family and domain databases

CDDicd00534. DHNA_DHNTPE. 2 hits.
cd00739. DHPS. 1 hit.
cd00483. HPPK. 1 hit.
Gene3Di3.20.20.20. 1 hit.
3.30.70.560. 1 hit.
InterProiIPR006390. DHP_synth.
IPR011005. Dihydropteroate_synth-like.
IPR006157. FolB_dom.
IPR016261. Folic_acid_synth.
IPR000550. Hppk.
IPR000489. Pterin-binding_dom.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.