Folic acid synthesis protein FOL1 (P53848)

Identification
NameFolic acid synthesis protein FOL1
Synonyms
  • Dihydroneopterin aldolase
  • DHNA
  • FASA
  • FASB
  • 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
  • 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
  • PPPK
  • 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
  • HPPK
  • FASC
  • Dihydropteroate synthase
  • DHPS
  • Dihydropteroate pyrophosphorylase
  • FASD
Gene NameFOL1
Enzyme Class
Biological Properties
General FunctionInvolved in dihydropteroate synthase activity
Specific FunctionCatalyzes three sequential steps of tetrahydrofolate biosynthesis
Cellular LocationMitochondrion membrane
SMPDB Pathways
tetrahydrofolate biosynthesisPW002417 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Folate biosynthesisec00790 Map00790
SMPDB Reactions
7,8-Dihydroneopterin → Glycolaldehyde + 2-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-ol
2-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-ol + Adenosine triphosphate → Adenosine monophosphate + hydron + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-Aminobenzoic acid → Pyrophosphate + 7,8-Dihydropteroic acid
KEGG Reactions
2-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-ol + Adenosine triphosphate → Adenosine monophosphate + (2-Amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl trihydrogen diphosphate + hydron
7,8-Dihydroneopterin → Glycolaldehyde + 2-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-ol
2-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-ol + 4-Aminobenzoic acid → water + 7,8-Dihydropteroic acid
(2-Amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl trihydrogen diphosphate + 4-Aminobenzoic acid → Pyrophosphate + 7,8-Dihydropteroic acid
Metabolites
YMDB IDNameView
YMDB00097Adenosine monophosphateShow
YMDB00109Adenosine triphosphateShow
YMDB001492-amino-6-(hydroxymethyl)-7,8-dihydropteridin-4-olShow
YMDB00219PyrophosphateShow
YMDB002937,8-Dihydropteroic acidShow
YMDB00343GlycolaldehydeShow
YMDB00356(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate(3-)Show
YMDB00430(2-Amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl trihydrogen diphosphateShow
YMDB004934-Aminobenzoic acidShow
YMDB005797,8-DihydroneopterinShow
YMDB006677,8-dihydropteroateShow
YMDB00845Dihydropterin-CH2OHShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB16254(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphateShow
GO Classification
Component
Not Available
Function
lyase activity
carbon-carbon lyase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
diphosphotransferase activity
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
aldehyde-lyase activity
dihydroneopterin aldolase activity
dihydropteroate synthase activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular metabolic process
cellular aromatic compound metabolic process
folic acid and derivative metabolic process
folic acid and derivative biosynthetic process
pteridine and derivative metabolic process
metabolic process
tetrahydrofolate biosynthetic process
Gene Properties
Chromosome Locationchromosome 14
LocusYNL256W
Gene Sequence>YNL256W FOL1 SGDID:S000005200, Chr XIV from 164623-167097, Verified ORF, "Multifunctional enzyme of the folic acid biosynthesis pathway, has dihydropteroate synthetase, dihydro-6-hydroxymethylpterin pyrophosphokinase, and dihydroneopterin aldolase activit ATGTCAAAGCTATTTTCTACTGTCAATTCTGCAAGACATAGTGTACCACTAGGCGGCATG AGAGATTATGTGCACATTAAGAAACTAGAGATGAATACAGTTCTTGGGCCTGATTCCTGG AATCAATTAATGCCTCAGAAATGTCTACTAAGCTTAGATATGGGTACAGATTTTAGTAAA TCTGCGGCTACGGATGATTTGAAATATTCTCTAAATTATGCAGTTATTTCTCGTGATTTG ACGAATTTCGTCAGCAAAAAAAAGAATTGGGGTTCTGTTTCTAATTTGGCTAAATCTGTG TCTCAATTTGTTATGGACAAATATTCTGGTGTCGAGTGTCTGAATTTAGAAGTGCAGGCG GATACAACGCATATTAGAAGTGACCACATATCTTGTATTATTCAACAAGAAAGAGGGAAT CCAGAATCACAGGAATTTGACGTTGTTAGGATATCTGAGTTAAAAATGTTGACTTTGATT GGTGTTTTCACCTTTGAGAGACTTAAGAAACAGTATGTAACTTTGGATATAAAGTTGCCT TGGCCAAAGAAAGCCGAATTGCCACCGCCAGTGCAAAGCATAATTGATAACGTTGTCAAG TTTGTGGAGGAATCAAATTTCAAGACTGTGGAAGCTCTTGTAGAATCTGTGTCAGCTGTT ATTGCCCATAACGAGTATTTTCAAAAGTTTCCAGATTCGCCTTTGGTGGTGAAGGTTTTG AAATTAAACGCAATCACAGCCACAGAAGGTGTTGGTGTAAGCTGTATTAGAGAGCCCAGG GAGATTGCGATGGTAAATATTCCATATCTTTCCTCCATACATGAATCGTCTGATATTAAG TTCCAATTGTCTTCATCACAAAACACTCCTATTGAGGGTAAAAATACATGGAAAAGAGCG TTTTTAGCGTTTGGTTCAAACATTGGGGACCGTTTCAAACACATTCAAATGGCGTTGCAA TTATTATCAAGGGAAAAAACGGTTAAATTACGGAATATTTCGTCTATTTTTGAAAGTGAA CCAATGTATTTCAAAGATCAAACCCCTTTCATGAATGGGTGTGTTGAGGTGGAGACATTA CTGACCCCAAGCGAATTATTAAAATTGTGTAAAAAAATTGAATATGAAGAGTTGCAAAGA GTCAAGCATTTTGATAATGGTCCGAGAACAATAGATCTGGATATTGTTATGTTTTTGAAT AGCGCCGGAGAAGATATTATAGTAAATGAACCGGATTTGAATATACCGCATCCTAGAATG CTGGAGAGGACTTTCGTTCTTGAGCCGTTATGTGAATTAATATCCCCCGTTCACCTTCAT CCTGTGACAGCGGAACCCATTGTAGACCATTTAAAACAGTTATACGACAAACAGCATGAT GAAGATACCTTATGGAAATTAGTTCCATTGCCTTATCGTAGTGGTGTGGAGCCTAGATTT TTGAAATTCAAGACCGCTACAAAACTTGACGAATTTACTGGAGAAACAAACAGAATTACT GTTTCACCTACATATATCATGGCTATCTTCAACGCTACACCAGATTCATTTTCCGATGGA GGTGAGCATTTTGCGGACATTGAAAGTCAATTGAATGATATCATTAAATTGTGTAAAGAC GCATTATATTTGCATGAGAGCGTCATCATCGACGTTGGAGGGTGTTCTACCAGGCCTAAC TCTATTCAGGCGTCTGAGGAAGAAGAAATACGCAGGTCTATCCCATTAATTAAGGCCATT AGAGAAAGCACTGAGTTACCGCAAGATAAAGTCATACTATCCATTGATACTTATCGTTCC AATGTCGCTAAAGAAGCGATTAAAGTTGGAGTGGATATTATTAATGATATTTCGGGAGGT TTATTTGACAGCAACATGTTTGCCGTAATTGCAGAGAACCCAGAAATTTGTTATATTTTA TCACACACACGTGGTGATATTTCAACGATGAATAGGCTGGCGCATTACGAAAATTTTGCA TTGGGTGATTCTATTCAGCAAGAATTTGTTCATAATACCGACATTCAGCAGCTAGACGAC TTGAAAGACAAAACAGTGTTAATCAGGAATGTTGGTCAAGAAATTGGCGAAAGGTATATC AAAGCGATTGATAATGGAGTAAAGCGCTGGCAAATTCTAATCGACCCTGGACTTGGTTTT GCTAAGACCTGGAAGCAAAACTTACAAATTATTAGACATATCCCCATTTTAAAGAACTAC TCATTCACCATGAACTCAAACAATTCGCAAGTGTATGTTAACCTCAGAAATATGCCCGTT TTATTGGGTCCATCGCGCAAAAAATTCATTGGACATATCACAAAAGATGTGGATGCGAAG CAAAGAGACTTTGCTACTGGAGCGGTGGTAGCGTCGTGTATTGGTTTCGGCAGCGACATG GTTAGGGTCCATGACGTTAAAAATTGTTCGAAGAGCATTAAATTAGCAGATGCTATTTAT AAAGGTTTGGAATAA
Protein Properties
Pfam Domain Function
Protein Residues824
Protein Molecular Weight93119.10156
Protein Theoretical pI6.4
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Folic acid synthesis protein FOL1 MSKLFSTVNSARHSVPLGGMRDYVHIKKLEMNTVLGPDSWNQLMPQKCLLSLDMGTDFSK SAATDDLKYSLNYAVISRDLTNFVSKKKNWGSVSNLAKSVSQFVMDKYSGVECLNLEVQA DTTHIRSDHISCIIQQERGNPESQEFDVVRISELKMLTLIGVFTFERLKKQYVTLDIKLP WPKKAELPPPVQSIIDNVVKFVEESNFKTVEALVESVSAVIAHNEYFQKFPDSPLVVKVL KLNAITATEGVGVSCIREPREIAMVNIPYLSSIHESSDIKFQLSSSQNTPIEGKNTWKRA FLAFGSNIGDRFKHIQMALQLLSREKTVKLRNISSIFESEPMYFKDQTPFMNGCVEVETL LTPSELLKLCKKIEYEELQRVKHFDNGPRTIDLDIVMFLNSAGEDIIVNEPDLNIPHPRM LERTFVLEPLCELISPVHLHPVTAEPIVDHLKQLYDKQHDEDTLWKLVPLPYRSGVEPRF LKFKTATKLDEFTGETNRITVSPTYIMAIFNATPDSFSDGGEHFADIESQLNDIIKLCKD ALYLHESVIIDVGGCSTRPNSIQASEEEEIRRSIPLIKAIRESTELPQDKVILSIDTYRS NVAKEAIKVGVDIINDISGGLFDSNMFAVIAENPEICYILSHTRGDISTMNRLAHYENFA LGDSIQQEFVHNTDIQQLDDLKDKTVLIRNVGQEIGERYIKAIDNGVKRWQILIDPGLGF AKTWKQNLQIIRHIPILKNYSFTMNSNNSQVYVNLRNMPVLLGPSRKKFIGHITKDVDAK QRDFATGAVVASCIGFGSDMVRVHDVKNCSKSIKLADAIYKGLE
References
External Links
ResourceLink
Saccharomyces Genome Database FOL1
Uniprot IDP53848
Uniprot NameFOL1_YEAST
General Reference
  • Sen-Gupta, M., Guldener, U., Beinhauer, J., Fiedler, T., Hegemann, J. H. (1997). "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the left arm of chromosome XIV from Saccharomyces cerevisiae." Yeast 13:849-860.9234673
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  • Zhang, Z., Dietrich, F. S. (2005). "Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE." Nucleic Acids Res 33:2838-2851.15905473
  • Kellis, M., Patterson, N., Endrizzi, M., Birren, B., Lander, E. S. (2003). "Sequencing and comparison of yeast species to identify genes and regulatory elements." Nature 423:241-254.12748633
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278
  • Guldener, U., Koehler, G. J., Haussmann, C., Bacher, A., Kricke, J., Becher, D., Hegemann, J. H. (2004). "Characterization of the Saccharomyces cerevisiae Fol1 protein: starvation for C1 carrier induces pseudohyphal growth." Mol Biol Cell 15:3811-3828.15169867
  • Calvert, M. E., Keck, K. M., Ptak, C., Shabanowitz, J., Hunt, D. F., Pemberton, L. F. (2008). "Phosphorylation by casein kinase 2 regulates Nap1 localization and function." Mol Cell Biol 28:1313-1325.18086883
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Lawrence, M. C., Iliades, P., Fernley, R. T., Berglez, J., Pilling, P. A., Macreadie, I. G. (2005). "The three-dimensional structure of the bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase of Saccharomyces cerevisiae." J Mol Biol 348:655-670.15826662