Folylpolyglutamate synthase
Details
- Name
- Folylpolyglutamate synthase
- Synonyms
- 6.3.2.17
- Folylpoly-gamma-glutamate synthetase
- FPGS
- Tetrahydrofolate synthase
- Tetrahydrofolylpolyglutamate synthase
- Gene Name
- fgs
- Organism
- Lactobacillus casei
- Amino acid sequence
>lcl|BSEQ0016452|Folylpolyglutamate synthase MNYTETVAYIHSFPRLAKTGDHRRILTLLHALGNPQQQGRYIHVTGTNGKGSAANAIAHV LEASGLTVGLYTSPFIMRFNERIMIDHEPIPDAALVNAVAFVRAALERLQQQQADFNVTE FEFITALGYWYFRQRQVDVAVIEVGIGGDTDSTNVITPVVSVLTEVALDHQKLLGHTITA IAKHKAGIIKRGIPVVTGNLVPDAAAVVAAKVATTGSQWLRFDRDFSVPKAKLHGWGQRF TYEDQDGRISDLEVPLVGDYQQRNMAIAIQTAKVYAKQTEWPLTPQNIRQGLAASHWPAR LEKISDTPLIVIDGAHNPDGINGLITALKQLFSQPITVIAGILADKDYAAMADRLTAAFS TVYLVPVPGTPRALPEAGYEALHEGRLKDSWQEALAASLNDVPDQPIVITGSLYLASAVR QTLLGGKS
- Number of residues
- 428
- Molecular Weight
- 46588.815
- Theoretical pI
- 7.02
- GO Classification
- FunctionsATP binding / tetrahydrofolylpolyglutamate synthase activityProcessesone-carbon metabolic process
- General Function
- Tetrahydrofolylpolyglutamate synthase activity
- Specific Function
- Conversion of folates to polyglutamate derivatives. It prefers 5,10-methylenetetrahydrofolate, rather than 10-formyltetrahydrofolate as folate substrate.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0002961|1287 bp ATGAATTACACAGAAACGGTTGCCTACATTCATTCTTTTCCGCGTTTGGCCAAGACCGGT GACCATCGGCGGATTTTAACGTTATTACATGCACTCGGCAATCCGCAGCAACAAGGGCGG TATATTCACGTGACTGGTACTAATGGAAAAGGCTCAGCCGCTAATGCGATTGCACATGTC CTTGAGGCAAGCGGTTTGACAGTCGGGTTATATACCTCGCCGTTTATCATGCGGTTTAAT GAACGGATCATGATTGACCATGAACCGATTCCGGATGCTGCGTTAGTCAATGCGGTTGCG TTTGTCAGGGCTGCACTGGAGCGGCTTCAGCAGCAACAAGCTGATTTTAACGTGACGGAA TTTGAATTCATTACCGCGCTGGGCTATTGGTATTTTCGTCAGCGTCAGGTTGATGTTGCG GTGATTGAAGTCGGTATTGGCGGCGACACGGATTCGACCAATGTCATCACGCCGGTTGTC AGTGTTTTGACCGAGGTTGCTTTAGATCACCAGAAGTTGCTGGGGCATACGATTACGGCG ATTGCCAAGCATAAGGCCGGTATTATCAAACGGGGTATTCCGGTTGTAACCGGTAACTTG GTGCCGGATGCTGCTGCCGTTGTCGCAGCCAAGGTCGCGACAACAGGGAGTCAATGGTTG CGTTTTGACCGCGATTTTTCGGTTCCTAAGGCTAAGCTTCACGGTTGGGGCCAACGGTTT ACTTATGAAGACCAAGATGGACGTATTAGTGATTTGGAGGTGCCGTTGGTTGGCGATTAC CAGCAACGTAATATGGCAATTGCGATTCAAACGGCAAAAGTGTATGCCAAGCAGACAGAA TGGCCTTTGACGCCCCAGAATATTCGCCAAGGGCTTGCTGCCAGTCATTGGCCAGCCCGA CTCGAAAAGATAAGTGATACGCCTTTGATCGTCATTGACGGGGCGCACAATCCGGATGGC ATCAATGGTTTGATTACGGCGCTAAAGCAACTTTTTTCCCAACCCATTACTGTTATTGCC GGCATCTTGGCGGATAAAGACTATGCGGCGATGGCGGATAGGCTGACCGCGGCATTTTCC ACGGTTTATCTGGTTCCGGTGCCGGGGACGCCGCGCGCCTTGCCTGAGGCTGGTTATGAG GCGCTGCACGAAGGTCGGTTAAAGGATTCGTGGCAGGAAGCATTGGCGGCGAGTCTTAAT GATGTGCCGGATCAGCCGATTGTGATCACCGGTTCGCTGTATTTAGCCTCAGCTGTTCGT CAAACTTTATTAGGGGGAAAATCATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P15925 UniProtKB Entry Name FOLC_LACCA GenBank Protein ID 149542 GenBank Gene ID J05221 - General References
- Toy J, Bognar AL: Cloning and expression of the gene encoding Lactobacillus casei folylpoly-gamma-glutamate synthetase in Escherichia coli and determination of its primary structure. J Biol Chem. 1990 Feb 15;265(5):2492-9. [Article]
- Sun X, Bognar AL, Baker EN, Smith CA: Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6647-52. [Article]
- Sun X, Cross JA, Bognar AL, Baker EN, Smith CA: Folate-binding triggers the activation of folylpolyglutamate synthetase. J Mol Biol. 2001 Jul 27;310(5):1067-78. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02301 5,10-Methylene-6-Hydrofolic Acid experimental unknown Details DB03755 Adenosine-5'-[Beta, Gamma-Methylene]Tetraphosphate experimental unknown Details DB03801 Lysine Nz-Carboxylic Acid experimental unknown Details DB03909 Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate experimental unknown Details