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Protein

Folic acid synthesis protein fol1

Gene

fol1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes three sequential steps of tetrahydrofolate biosynthesis.By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.By similarity

Pathway: 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.

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi472 – 4721MagnesiumBy similarity
Binding sitei480 – 4801SubstrateBy similarity
Binding sitei546 – 5461SubstrateBy similarity
Binding sitei565 – 5651SubstrateBy similarity
Binding sitei637 – 6371SubstrateBy similarity
Binding sitei677 – 6771SubstrateBy similarity
Binding sitei712 – 7121SubstrateBy similarity
Binding sitei714 – 7141SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Kinase, Lyase, Transferase

Keywords - Biological processi

Folate biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

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
ORF Names:SPBC1734.03, SPBC337.19
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1734.03.
PomBaseiSPBC1734.03.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitochondrion Source: PomBase

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Folic acid synthesis protein fol1PRO_0000343164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei281 – 2811Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ4LB35.

Interactioni

Protein-protein interaction databases

STRINGi4896.SPBC1734.03.1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini465 – 724260Pterin-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 167113DHNA 1Add
BLAST
Regioni179 – 27799DHNA 2Add
BLAST
Regioni295 – 454160HPKAdd
BLAST
Regioni457 – 733277DHPSAdd
BLAST
Regioni511 – 5122Substrate bindingBy similarity

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.
InParanoidiQ4LB35.
KOiK13939.
OMAiFRNGPRA.
OrthoDBiEOG7RZ5ZF.

Family and domain databases

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.
[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. 1 hit.
SSF55083. SSF55083. 1 hit.
TIGRFAMsiTIGR01496. DHPS. 1 hit.
TIGR01498. folK. 1 hit.
PROSITEiPS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4LB35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLVNLWGI YPFIRNNSLH GFAKIPRIVS TIPRQLRFSS LRHPTRQMDL
60 70 80 90 100
IHDTVVVENL NTFAVVGQDQ WKRKEPQPVQ IDVYMRNNVQ LAGEKDELKS
110 120 130 140 150
TIHYGIASKL LRKEIEGSFF TTPKDLVNKI ASLCFEDVID TSHVSIKLTL
160 170 180 190 200
PKCVLRSKNG LHYYAERERN STSNFVDRIE FSDLELATIL GIHAFERQEK
210 220 230 240 250
QRVCLNISFA NTEVEALEIA RAIAEYVEQS AFLTIEALVV NLSKYLCFTK
260 270 280 290 300
NLDDISIKAE KPSAITFANA SAVQIYRTRS YFLQESLHKY ESTKNKIAYL
310 320 330 340 350
SFGSNIGDKF EQIQTALSML HKIEGIRVLD VSPLYETEPM YYKDQPSFLN
360 370 380 390 400
GVCKIETRMS PINLLRACQS IEQEMGRIKT ILKGPRCIDL DIVLYEDCVY
410 420 430 440 450
ESEVLTIPHL GLQEREFVLR PLLALSPDLV HPYTHQPLQE ALDKLPSQGI
460 470 480 490 500
RLYSSFDNKK IINGALTMGI LNVTPDSFSD GGKVSQNNIL EKAKSMVGDG
510 520 530 540 550
ASILDIGGQS TKPGADPVSV EEELRRVIPM ISLLRSSGIT VPISIDTYYS
560 570 580 590 600
KVAKLAIEAG ANIINDVTGG MGDEKMLPLA ASLQVPICIM HMRGTPETMK
610 620 630 640 650
ALSIYEKDIV EEVAVELSSR VEAAVQSGVH RYNIILDPGF GFAKTPKQSA
660 670 680 690 700
GLLGRLHELM KKPQFKDMHW LSGPSRKGFT GYFTGDASPK DRIWGTSACV
710 720 730
TASVLQGVSI VRVHDTKEMS KVVGMANAIR YVP
Length:733
Mass (Da):81,926
Last modified:October 3, 2012 - v2
Checksum:iA4401685D5ACF5CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21289.2.
PIRiT39650.
RefSeqiNP_595420.2. NM_001021327.2.

Genome annotation databases

EnsemblFungiiSPBC1734.03.1; SPBC1734.03.1:pep; SPBC1734.03.
GeneIDi2539851.
KEGGispo:SPBC1734.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21289.2.
PIRiT39650.
RefSeqiNP_595420.2. NM_001021327.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4896.SPBC1734.03.1.

Proteomic databases

MaxQBiQ4LB35.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1734.03.1; SPBC1734.03.1:pep; SPBC1734.03.
GeneIDi2539851.
KEGGispo:SPBC1734.03.

Organism-specific databases

EuPathDBiFungiDB:SPBC1734.03.
PomBaseiSPBC1734.03.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217511.
InParanoidiQ4LB35.
KOiK13939.
OMAiFRNGPRA.
OrthoDBiEOG7RZ5ZF.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00154.
UPA00077; UER00155.
UPA00077; UER00156.

Miscellaneous databases

NextBioi20800998.
PROiQ4LB35.

Family and domain databases

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.
[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. 1 hit.
SSF55083. SSF55083. 1 hit.
TIGRFAMsiTIGR01496. DHPS. 1 hit.
TIGR01498. folK. 1 hit.
PROSITEiPS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFOL1_SCHPO
AccessioniPrimary (citable) accession number: Q4LB35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: October 3, 2012
Last modified: June 24, 2015
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.