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Q4LB35 (FOL1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names:SPBC1734.03, SPBC337.19
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes three sequential steps of tetrahydrofolate biosynthesis By similarity.

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.

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

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

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.

Subcellular location

Cytoplasm Ref.3.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 733733Folic acid synthesis protein fol1
PRO_0000343164

Regions

Domain465 – 724260Pterin-binding
Region55 – 167113DHNA 1
Region179 – 27799DHNA 2
Region295 – 454160HPK
Region457 – 733277DHPS
Region511 – 5122Substrate binding By similarity

Sites

Metal binding4721Magnesium By similarity
Binding site4801Substrate By similarity
Binding site5461Substrate By similarity
Binding site5651Substrate By similarity
Binding site6371Substrate By similarity
Binding site6771Substrate By similarity
Binding site7121Substrate By similarity
Binding site7141Substrate By similarity

Amino acid modifications

Modified residue2811Phosphotyrosine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q4LB35 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: A4401685D5ACF5CF

FASTA73381,926
        10         20         30         40         50         60 
MKSLVNLWGI YPFIRNNSLH GFAKIPRIVS TIPRQLRFSS LRHPTRQMDL IHDTVVVENL 

        70         80         90        100        110        120 
NTFAVVGQDQ WKRKEPQPVQ IDVYMRNNVQ LAGEKDELKS TIHYGIASKL LRKEIEGSFF 

       130        140        150        160        170        180 
TTPKDLVNKI ASLCFEDVID TSHVSIKLTL PKCVLRSKNG LHYYAERERN STSNFVDRIE 

       190        200        210        220        230        240 
FSDLELATIL GIHAFERQEK QRVCLNISFA NTEVEALEIA RAIAEYVEQS AFLTIEALVV 

       250        260        270        280        290        300 
NLSKYLCFTK NLDDISIKAE KPSAITFANA SAVQIYRTRS YFLQESLHKY ESTKNKIAYL 

       310        320        330        340        350        360 
SFGSNIGDKF EQIQTALSML HKIEGIRVLD VSPLYETEPM YYKDQPSFLN GVCKIETRMS 

       370        380        390        400        410        420 
PINLLRACQS IEQEMGRIKT ILKGPRCIDL DIVLYEDCVY ESEVLTIPHL GLQEREFVLR 

       430        440        450        460        470        480 
PLLALSPDLV HPYTHQPLQE ALDKLPSQGI RLYSSFDNKK IINGALTMGI LNVTPDSFSD 

       490        500        510        520        530        540 
GGKVSQNNIL EKAKSMVGDG ASILDIGGQS TKPGADPVSV EEELRRVIPM ISLLRSSGIT 

       550        560        570        580        590        600 
VPISIDTYYS KVAKLAIEAG ANIINDVTGG MGDEKMLPLA ASLQVPICIM HMRGTPETMK 

       610        620        630        640        650        660 
ALSIYEKDIV EEVAVELSSR VEAAVQSGVH RYNIILDPGF GFAKTPKQSA GLLGRLHELM 

       670        680        690        700        710        720 
KKPQFKDMHW LSGPSRKGFT GYFTGDASPK DRIWGTSACV TASVLQGVSI VRVHDTKEMS 

       730 
KVVGMANAIR YVP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA21289.2.
PIRT39650.
RefSeqNP_595420.2. NM_001021327.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4896.SPBC1734.03-1.

Proteomic databases

MaxQBQ4LB35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1734.03.1; SPBC1734.03.1:pep; SPBC1734.03.
GeneID2539851.
KEGGspo:SPBC1734.03.

Organism-specific databases

PomBaseSPBC1734.03.

Phylogenomic databases

eggNOGCOG0294.
HOGENOMHOG000217511.
KOK13939.
OrthoDBEOG7RZ5ZF.

Enzyme and pathway databases

UniPathwayUPA00077; UER00154.
UPA00077; UER00155.
UPA00077; UER00156.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
3.30.70.560. 1 hit.
InterProIPR006390. DHP_synth.
IPR011005. 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. 1 hit.
SSF55083. SSF55083. 1 hit.
TIGRFAMsTIGR01496. DHPS. 1 hit.
TIGR01498. folK. 1 hit.
PROSITEPS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800998.

Entry information

Entry nameFOL1_SCHPO
AccessionPrimary (citable) accession number: Q4LB35
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: October 3, 2012
Last modified: June 11, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways