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Q4LB35

- FOL1_SCHPO

UniProt

Q4LB35 - FOL1_SCHPO

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Protein

Folic acid synthesis protein fol1

Gene
fol1, SPBC1734.03, SPBC337.19
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes three sequential steps of tetrahydrofolate biosynthesis By similarity.

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.
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.

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi472 – 4721Magnesium By similarity
Binding sitei480 – 4801Substrate By similarity
Binding sitei546 – 5461Substrate By similarity
Binding sitei565 – 5651Substrate By similarity
Binding sitei637 – 6371Substrate By similarity
Binding sitei677 – 6771Substrate By similarity
Binding sitei712 – 7121Substrate By similarity
Binding sitei714 – 7141Substrate By similarity

GO - Molecular functioni

  1. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Source: PomBase
  2. ATP binding Source: UniProtKB-KW
  3. dihydroneopterin aldolase activity Source: PomBase
  4. dihydropteroate synthase activity Source: PomBase
  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: UniProtKB-UniPathway
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

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: Chromosome II

Organism-specific databases

PomBaseiSPBC1734.03.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. mitochondrion Source: PomBase
Complete GO annotation...

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-bindingAdd
BLAST

Region

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

Sequence similaritiesi

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.

Phylogenomic databases

eggNOGiCOG0294.
HOGENOMiHOG000217511.
KOiK13939.
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

MKSLVNLWGI YPFIRNNSLH GFAKIPRIVS TIPRQLRFSS LRHPTRQMDL    50
IHDTVVVENL NTFAVVGQDQ WKRKEPQPVQ IDVYMRNNVQ LAGEKDELKS 100
TIHYGIASKL LRKEIEGSFF TTPKDLVNKI ASLCFEDVID TSHVSIKLTL 150
PKCVLRSKNG LHYYAERERN STSNFVDRIE FSDLELATIL GIHAFERQEK 200
QRVCLNISFA NTEVEALEIA RAIAEYVEQS AFLTIEALVV NLSKYLCFTK 250
NLDDISIKAE KPSAITFANA SAVQIYRTRS YFLQESLHKY ESTKNKIAYL 300
SFGSNIGDKF EQIQTALSML HKIEGIRVLD VSPLYETEPM YYKDQPSFLN 350
GVCKIETRMS PINLLRACQS IEQEMGRIKT ILKGPRCIDL DIVLYEDCVY 400
ESEVLTIPHL GLQEREFVLR PLLALSPDLV HPYTHQPLQE ALDKLPSQGI 450
RLYSSFDNKK IINGALTMGI LNVTPDSFSD GGKVSQNNIL EKAKSMVGDG 500
ASILDIGGQS TKPGADPVSV EEELRRVIPM ISLLRSSGIT VPISIDTYYS 550
KVAKLAIEAG ANIINDVTGG MGDEKMLPLA ASLQVPICIM HMRGTPETMK 600
ALSIYEKDIV EEVAVELSSR VEAAVQSGVH RYNIILDPGF GFAKTPKQSA 650
GLLGRLHELM KKPQFKDMHW LSGPSRKGFT GYFTGDASPK DRIWGTSACV 700
TASVLQGVSI VRVHDTKEMS KVVGMANAIR YVP 733
Length:733
Mass (Da):81,926
Last modified:October 3, 2012 - v2
Checksum:iA4401685D5ACF5CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAA21289.2 .
PIRi T39650.
RefSeqi NP_595420.2. NM_001021327.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4896.SPBC1734.03-1.

Proteomic databases

MaxQBi Q4LB35.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC1734.03.1 ; SPBC1734.03.1:pep ; SPBC1734.03 .
GeneIDi 2539851.
KEGGi spo:SPBC1734.03.

Organism-specific databases

PomBasei SPBC1734.03.

Phylogenomic databases

eggNOGi COG0294.
HOGENOMi HOG000217511.
KOi K13939.
OrthoDBi EOG7RZ5ZF.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00154 .
UPA00077 ; UER00155 .
UPA00077 ; UER00156 .

Miscellaneous databases

NextBioi 20800998.

Family and domain databases

Gene3Di 3.20.20.20. 1 hit.
3.30.70.560. 1 hit.
InterProi IPR006390. DHP_synth.
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. 1 hit.
SSF55083. SSF55083. 1 hit.
TIGRFAMsi TIGR01496. DHPS. 1 hit.
TIGR01498. folK. 1 hit.
PROSITEi PS00793. DHPS_2. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 11, 2014
This is version 62 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

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