ID FOL1_SCHPO Reviewed; 733 AA.
AC Q4LB35;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 01-MAY-2013, entry version 55.
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=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase;
DE Short=PPPK;
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase;
DE Short=HPPK;
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 (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales;
OC Schizosaccharomycetaceae; Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, 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 -!- COFACTOR: Binds 1 magnesium ion per subunit. Magnesium is required
CC for activity, even if it interacts primarily with the substrate
CC (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
CC from 7,8-dihydroneopterin triphosphate: step 3/4.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
CC amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
CC from 7,8-dihydroneopterin triphosphate: step 4/4.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
CC 7,8-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; CAA21289.2; -; Genomic_DNA.
DR PIR; T39650; T39650.
DR RefSeq; NP_595420.2; NM_001021327.2.
DR STRING; 4896.SPBC1734.03-1; -.
DR GeneID; 2539851; -.
DR KEGG; spo:SPBC1734.03; -.
DR PomBase; SPBC1734.03; -.
DR eggNOG; COG0294; -.
DR HOGENOM; HOG000217511; -.
DR KO; K13939; -.
DR OrthoDB; EOG4CJZRP; -.
DR UniPathway; UPA00077; UER00154.
DR UniPathway; UPA00077; UER00155.
DR UniPathway; UPA00077; UER00156.
DR NextBio; 20800998; -.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; ISS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; ISS:PomBase.
DR GO; GO:0004156; F:dihydropteroate synthase activity; ISS:PomBase.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.30.70.560; -; 1.
DR InterPro; IPR006390; DHP_synth.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR016261; Folic_acid_synth.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR000489; Pterin-binding.
DR Pfam; PF02152; FolB; 2.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR PIRSF; PIRSF000741; Folic_acid_synth; 1.
DR SMART; SM00905; FolB; 2.
DR SUPFAM; SSF51717; DHP_synth_like; 1.
DR SUPFAM; SSF55083; Hppk; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
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; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1 733 Folic acid synthesis protein fol1.
FT /FTId=PRO_0000343164.
FT DOMAIN 465 724 Pterin-binding.
FT REGION 55 167 DHNA 1.
FT REGION 179 277 DHNA 2.
FT REGION 295 454 HPK.
FT REGION 457 733 DHPS.
FT REGION 511 512 Substrate binding (By similarity).
FT METAL 472 472 Magnesium (By similarity).
FT BINDING 480 480 Substrate (By similarity).
FT BINDING 546 546 Substrate (By similarity).
FT BINDING 565 565 Substrate (By similarity).
FT BINDING 637 637 Substrate (By similarity).
FT BINDING 677 677 Substrate (By similarity).
FT BINDING 712 712 Substrate (By similarity).
FT BINDING 714 714 Substrate (By similarity).
FT MOD_RES 281 281 Phosphotyrosine.
SQ SEQUENCE 733 AA; 81926 MW; A4401685D5ACF5CF CRC64;
MKSLVNLWGI YPFIRNNSLH GFAKIPRIVS TIPRQLRFSS LRHPTRQMDL IHDTVVVENL
NTFAVVGQDQ WKRKEPQPVQ IDVYMRNNVQ LAGEKDELKS TIHYGIASKL LRKEIEGSFF
TTPKDLVNKI ASLCFEDVID TSHVSIKLTL PKCVLRSKNG LHYYAERERN STSNFVDRIE
FSDLELATIL GIHAFERQEK QRVCLNISFA NTEVEALEIA RAIAEYVEQS AFLTIEALVV
NLSKYLCFTK NLDDISIKAE KPSAITFANA SAVQIYRTRS YFLQESLHKY ESTKNKIAYL
SFGSNIGDKF EQIQTALSML HKIEGIRVLD VSPLYETEPM YYKDQPSFLN GVCKIETRMS
PINLLRACQS IEQEMGRIKT ILKGPRCIDL DIVLYEDCVY ESEVLTIPHL GLQEREFVLR
PLLALSPDLV HPYTHQPLQE ALDKLPSQGI RLYSSFDNKK IINGALTMGI LNVTPDSFSD
GGKVSQNNIL EKAKSMVGDG ASILDIGGQS TKPGADPVSV EEELRRVIPM ISLLRSSGIT
VPISIDTYYS KVAKLAIEAG ANIINDVTGG MGDEKMLPLA ASLQVPICIM HMRGTPETMK
ALSIYEKDIV EEVAVELSSR VEAAVQSGVH RYNIILDPGF GFAKTPKQSA GLLGRLHELM
KKPQFKDMHW LSGPSRKGFT GYFTGDASPK DRIWGTSACV TASVLQGVSI VRVHDTKEMS
KVVGMANAIR YVP
//
