Reviewed, UniProtKB/Swiss-Prot Q4LB35 (FOL1_SCHPO)

Names and origin

Protein names

Recommended name:
    Folic acid synthesis protein fol1
Including the following 3 domains:
    1- Recommended name:
            Dihydroneopterin aldolase
                Short name=DHNA
              EC=4.1.2.25
        Alternative name(s):
            FASA
            FASB
    2- Recommended name:
            2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
              EC=2.7.6.3
        Alternative name(s):
            7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
              Short name=HPPK
            6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
              Short name=PPPK
            FASC
    3- Recommended name:
            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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	686 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate: step 3/4. Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate: step 4/4. Cofactor biosynthesis; tetrahydrofolate biosynthesis; dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Subcellular location	Cytoplasm. Ref.2
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.

Ontologies

Keywords
Biological process	Folate biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Lyase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW dihydroneopterin aldolase activity Inferred from electronic annotation. Source: EC dihydropteroate synthase activity Inferred from electronic annotation. Source: EC kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 686	686	Folic acid synthesis protein fol1		PRO_0000343164
Regions
	Domain	418 – 677	260	Pterin-binding
	Region	8 – 121	114	DHNA 1
	Region	132 – 232	101	DHNA 2
	Region	252 – 379	128	HPK
	Region	410 – 686	277	DHPS
Amino acid modifications
	Modified residue	234	1	Phosphotyrosine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q4LB35-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: C0D8287AAB5F338B	FASTA	686	76,396
	10 20 30 40 50 60 MDLIHDTVVV ENLNTFAVVG QDQWKRKEPQ PVQIDVYMRN NVQLAGEKDE LKSTIHYGIA 70 80 90 100 110 120 SKLLRKEIEG SFFTTPKDLV NKIASLCFED VIDTSHVSIK LTLPKCVLRS KNGLHYYAER 130 140 150 160 170 180 ERNSTSNFVD RIEFSDLELA TILGIHAFER QEKQRVCLNI SFANTEVEAL EIARAIAEYV 190 200 210 220 230 240 EQSAFLTIEA LVVNLSKYLC FTKNLDDISI KAEKPSAITF ANASAVQIYR TRSYFLQESL 250 260 270 280 290 300 HKYESTKNKI AYLSFGSNIG DKFEQIQTAL SMLHKIEGIR VLDVSPLYET EPMYYKDQPS 310 320 330 340 350 360 FLNGVCKIET RMSPINLLRA CQSIEQEMGR IKTILKGPRC IDLDIVLYED CVYESEVLTI 370 380 390 400 410 420 PHLGLQEREF VLRPLLALSP DLVHPYTHQP LQEALDKLPS QGIRLYSSFD NKKIINGALT 430 440 450 460 470 480 MGILNVTPDS FSDGGKVSQN NILEKAKSMV GDGASILDIG GQSTKPGADP VSVEEELRRV 490 500 510 520 530 540 IPMISLLRSS GITVPISIDT YYSKVAKLAI EAGANIINDV TGGMGDEKML PLAASLQVPI 550 560 570 580 590 600 CIMHMRGTPE TMKALSIYEK DIVEEVAVEL SSRVEAAVQS GVHRYNIILD PGFGFAKTPK 610 620 630 640 650 660 QSAGLLGRLH ELMKKPQFKD MHWLSGPSRK GFTGYFTGDA SPKDRIWGTS ACVTASVLQG 670 680 VSIVRVHDTK EMSKVVGMAN AIRYVP

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. , 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"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: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA21289.1.
PIR	T39650.
RefSeq	NP_595420.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2539851.
KEGG	spo:SPBC1734.03.
NMPDR	fig|4896.1.peg.1286.
Organism-specific databases
GeneDB_Spombe	SPBC1734.03.
Phylogenomic databases
OMA	Q4LB35. GVFTFER.
Family and domain databases
InterPro	IPR000489. Dhdropt_synth. IPR006390. DHP_synth. IPR006157. FolB. IPR016261. Folic_acid_synth. IPR000550. Hppk. [Graphical view]
Gene3D	G3DSA:3.20.20.20. Dhdropt_synth. 1 hit. G3DSA:3.30.70.560. Hppk. 1 hit.
PANTHER	PTHR20941:SF1. DHP_synth. 1 hit.
Pfam	PF02152. FolB. 2 hits. PF01288. HPPK. 1 hit. PF00809. Pterin_bind. 1 hit. [Graphical view]
PIRSF	PIRSF000741. Folic_acid_synth. 1 hit.
TIGRFAMs	TIGR01496. DHPS. 1 hit. TIGR00526. folB_dom. 2 hits. TIGR01498. folK. 1 hit.
PROSITE	PS00792. DHPS_1. False negative. PS00793. DHPS_2. 1 hit. PS00794. HPPK. False negative. PS50972. PTERIN_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FOL1_SCHPO

Accession

Primary (citable) accession number: Q4LB35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	August 21, 2007
Last modified:	June 16, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)