ID FOL1_SCHPO Reviewed; 686 AA. AC Q4LB35; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 16-JUN-2009, entry version 18. DE RecName: Full=Folic acid synthesis protein fol1; DE Includes: DE RecName: Full=Dihydroneopterin aldolase; DE Short=DHNA; DE EC=4.1.2.25; DE AltName: Full=FASA; DE AltName: Full=FASB; DE Includes: DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; DE EC=2.7.6.3; DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; DE Short=HPPK; DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; DE Short=PPPK; DE AltName: Full=FASC; DE Includes: DE RecName: Full=Dihydropteroate synthase; DE Short=DHPS; DE EC=2.5.1.15; DE AltName: Full=Dihydropteroate pyrophosphorylase; DE AltName: Full=FASD; GN Name=fol1; ORFNames=SPBC1734.03, SPBC337.19; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=16823372; DOI=10.1038/nbt1222; RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., RA Yoshida M.; RT "ORFeome cloning and global analysis of protein localization in the RT fission yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234, AND MASS RP SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- FUNCTION: Catalyzes three sequential steps of tetrahydrofolate CC biosynthesis (By similarity). CC -!- CATALYTIC ACTIVITY: 2-amino-4-hydroxy-6-(D-erythro-1,2,3- CC trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6- CC hydroxymethyl-7,8-dihydropteridine + glycolaldehyde. CC -!- CATALYTIC ACTIVITY: ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8- CC dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6- CC yl)methyl diphosphate. CC -!- CATALYTIC ACTIVITY: (2-amino-4-hydroxy-7,8-dihydropteridin-6- CC yl)methyl diphosphate + 4-aminobenzoate = diphosphate + CC dihydropteroate. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2- CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate CC from 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)- CC dihydropteridine triphosphate: step 3/4. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2- CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate CC from 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)- CC dihydropteridine triphosphate: step 4/4. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8- CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHNA family. CC -!- SIMILARITY: In the central section; belongs to the HPPK family. CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CU329671; CAA21289.1; -; Genomic_DNA. DR PIR; T39650; T39650. DR RefSeq; NP_595420.1; -. DR GeneID; 2539851; -. DR KEGG; spo:SPBC1734.03; -. DR NMPDR; fig|4896.1.peg.1286; -. DR GeneDB_Spombe; SPBC1734.03; -. DR OMA; Q4LB35; GVFTFER. DR GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe. DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropte...; IEA:EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:EC. DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:EC. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro. DR InterPro; IPR000489; Dhdropt_synth. DR InterPro; IPR006390; DHP_synth. DR InterPro; IPR006157; FolB. DR InterPro; IPR016261; Folic_acid_synth. DR InterPro; IPR000550; Hppk. DR Gene3D; G3DSA:3.20.20.20; Dhdropt_synth; 1. DR Gene3D; G3DSA:3.30.70.560; Hppk; 1. DR PANTHER; PTHR20941:SF1; DHP_synth; 1. DR Pfam; PF02152; FolB; 2. DR Pfam; PF01288; HPPK; 1. DR Pfam; PF00809; Pterin_bind; 1. DR PIRSF; PIRSF000741; Folic_acid_synth; 1. DR TIGRFAMs; TIGR01496; DHPS; 1. DR TIGRFAMs; TIGR00526; folB_dom; 2. DR TIGRFAMs; TIGR01498; folK; 1. DR PROSITE; PS00792; DHPS_1; FALSE_NEG. DR PROSITE; PS00793; DHPS_2; 1. DR PROSITE; PS00794; HPPK; FALSE_NEG. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Folate biosynthesis; KW Kinase; Lyase; Multifunctional enzyme; Nucleotide-binding; KW Phosphoprotein; Transferase. FT CHAIN 1 686 Folic acid synthesis protein fol1. FT /FTId=PRO_0000343164. FT DOMAIN 418 677 Pterin-binding. FT REGION 8 121 DHNA 1. FT REGION 132 232 DHNA 2. FT REGION 252 379 HPK. FT REGION 410 686 DHPS. FT MOD_RES 234 234 Phosphotyrosine. SQ SEQUENCE 686 AA; 76396 MW; C0D8287AAB5F338B CRC64; MDLIHDTVVV ENLNTFAVVG QDQWKRKEPQ PVQIDVYMRN NVQLAGEKDE LKSTIHYGIA SKLLRKEIEG SFFTTPKDLV NKIASLCFED VIDTSHVSIK LTLPKCVLRS KNGLHYYAER ERNSTSNFVD RIEFSDLELA TILGIHAFER QEKQRVCLNI SFANTEVEAL EIARAIAEYV EQSAFLTIEA LVVNLSKYLC FTKNLDDISI KAEKPSAITF ANASAVQIYR TRSYFLQESL HKYESTKNKI AYLSFGSNIG DKFEQIQTAL SMLHKIEGIR VLDVSPLYET EPMYYKDQPS FLNGVCKIET RMSPINLLRA CQSIEQEMGR IKTILKGPRC IDLDIVLYED CVYESEVLTI PHLGLQEREF VLRPLLALSP DLVHPYTHQP LQEALDKLPS QGIRLYSSFD NKKIINGALT MGILNVTPDS FSDGGKVSQN NILEKAKSMV GDGASILDIG GQSTKPGADP VSVEEELRRV IPMISLLRSS GITVPISIDT YYSKVAKLAI EAGANIINDV TGGMGDEKML PLAASLQVPI CIMHMRGTPE TMKALSIYEK DIVEEVAVEL SSRVEAAVQS GVHRYNIILD PGFGFAKTPK QSAGLLGRLH ELMKKPQFKD MHWLSGPSRK GFTGYFTGDA SPKDRIWGTS ACVTASVLQG VSIVRVHDTK EMSKVVGMAN AIRYVP //