Glycerol kinase
Details
- Name
- Glycerol kinase
- Kind
- protein
- Synonyms
- 2.7.1.30
- ATP:glycerol 3-phosphotransferase
- GK
- Glycerokinase
- Gene Name
- glpK
- UniProtKB Entry
- P0A6F3Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0011141|Glycerol kinase MTEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSST LVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDG LEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVH VTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPI SGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVN YALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPY ARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLM QFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTER NYRYAGWKKAVKRAMAWEEHDE
- Number of residues
- 502
- Molecular Weight
- 56230.375
- Theoretical pI
- 5.18
- GO Classification
- FunctionsATP binding / glycerol kinase activity / metal ion binding / zinc ion bindingProcessescellular response to DNA damage stimulus / glycerol catabolic process / glycerol metabolic process / glycerol-3-phosphate metabolic process / phosphorylationComponentscytoplasm / cytosol
- General Function
- Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP.
- Specific Function
- ATP binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011142|Glycerol kinase (glpK) ATGACTGAAAAAAAATATATCGTTGCGCTCGACCAGGGCACCACCAGCTCCCGCGCGGTC GTAATGGATCACGATGCCAATATCATTAGCGTGTCGCAGCGCGAATTTGAGCAAATCTAC CCAAAACCAGGTTGGGTAGAACACGACCCAATGGAAATCTGGGCCACCCAAAGCTCCACG CTGGTAGAAGTGCTGGCGAAAGCCGATATCAGTTCCGATCAAATTGCAGCTATCGGTATT ACGAACCAGCGTGAAACCACTATTGTCTGGGAAAAAGAAACCGGCAAGCCTATCTATAAC GCCATTGTCTGGCAGTGCCGTCGTACCGCAGAAATCTGCGAGCATTTAAAACGTGACGGT TTAGAAGATTATATCCGCAGCAATACCGGTCTGGTGATTGACCCGTACTTTTCTGGCACC AAAGTGAAGTGGATCCTCGACCATGTGGAAGGCTCTCGCGAGCGTGCACGTCGTGGTGAA TTGCTGTTTGGTACGGTTGATACGTGGCTTATCTGGAAAATGACTCAGGGCCGTGTCCAT GTGACCGATTACACCAACGCCTCTCGTACCATGTTGTTCAACATCCATACCCTGGACTGG GACGACAAAATGCTGGAAGTGCTGGATATTCCGCGCGAGATGCTGCCAGAAGTGCGTCGT TCTTCCGAAGTATACGGTCAGACTAACATTGGCGGCAAAGGCGGCACGCGTATTCCAATC TCCGGGATCGCCGGTGACCAGCAGGCCGCGCTGTTTGGTCAGTTGTGCGTGAAAGAAGGG ATGGCGAAGAACACCTATGGCACTGGCTGCTTTATGCTGATGAACACTGGCGAGAAAGCG GTGAAATCAGAAAACGGCCTGCTGACCACCATCGCCTGCGGCCCGACTGGCGAAGTGAAC TATGCGTTGGAAGGTGCGGTGTTTATGGCAGGCGCATCCATTCAGTGGCTGCGCGATGAA ATGAAGTTGATTAACGACGCCTACGATTCCGAATATTTCGCCACCAAAGTGCAAAACACC AATGGTGTGTATGTGGTTCCGGCATTTACCGGGCTGGGTGCGCCGTACTGGGACCCGTAT GCGCGCGGGGCGATTTTCGGTCTGACTCGTGGGGTGAACGCTAACCACATTATACGCGCG ACGCTGGAGTCTATTGCTTATCAGACGCGTGACGTGCTGGAAGCGATGCAGGCCGACTCT GGTATCCGTCTGCACGCCCTGCGCGTGGATGGTGGCGCAGTAGCAAACAATTTCCTGATG CAGTTCCAGTCCGATATTCTCGGCACCCGCGTTGAGCGCCCGGAAGTGCGCGAAGTCACC GCATTGGGTGCGGCCTATCTCGCAGGCCTGGCGGTTGGCTTCTGGCAGAACCTCGACGAG CTGCAAGAGAAAGCGGTGATTGAGCGCGAGTTCCGTCCAGGCATCGAAACCACTGAGCGT AATTACCGTTACGCAGGCTGGAAAAAAGCGGTTAAACGCGCGATGGCGTGGGAAGAACAC GACGAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A6F3 UniProtKB Entry Name GLPK_ECOLI GenBank Protein ID 146220 GenBank Gene ID M18393 PDB ID(s) 1BO5, 1BOT, 1BU6, 1BWF, 1GLA, 1GLB, 1GLC, 1GLD, 1GLE, 1GLF, 1GLJ, 1GLL, 3EZW KEGG ID ecj:JW3897 NCBI Gene ID 948423 - General References
- Pettigrew DW, Ma DP, Conrad CA, Johnson JR: Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. J Biol Chem. 1988 Jan 5;263(1):135-9. [Article]
- Weissenborn DL, Wittekindt N, Larson TJ: Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12. J Biol Chem. 1992 Mar 25;267(9):6122-31. [Article]
- Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Muramatsu S, Mizuno T: Nucleotide sequence of the region encompassing the glpKF operon and its upstream region containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 1989 Jun 12;17(11):4378. [Article]
- Gonzalez-Gil G, Bringmann P, Kahmann R: FIS is a regulator of metabolism in Escherichia coli. Mol Microbiol. 1996 Oct;22(1):21-9. [Article]
- Pettigrew DW, Liu WZ, Holmes C, Meadow ND, Roseman S: A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. J Bacteriol. 1996 May;178(10):2846-52. [Article]
- Zwaig N, Lin EC: Feedback inhibition of glycerol kinase, a catabolic enzyme in Escherichia coli. Science. 1966 Aug 12;153(3737):755-7. [Article]
- Hayashi SI, Lin EC: Purification and properties of glycerol kinase from Escherichia coli. J Biol Chem. 1967 Mar 10;242(5):1030-5. [Article]
- Thorner JW, Paulus H: Composition and subunit structure of glycerol kinase from Escherichia coli. J Biol Chem. 1971 Jun 25;246(12):3885-94. [Article]
- Thorner JW, Paulus H: Catalytic and allosteric properties of glycerol kinase from Escherichia coli. J Biol Chem. 1973 Jun 10;248(11):3922-32. [Article]
- de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 1. Kinetic evidence. Biochemistry. 1978 Nov 28;17(24):5134-40. [Article]
- de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidence. Biochemistry. 1978 Nov 28;17(24):5141-6. [Article]
- de Riel JK, Paulus H: Subunit dissociation in the allosteric regulation of Glycerol kinase from Escherichia coli. 3. Role in desensitization. Biochemistry. 1978 Nov 28;17(24):5146-50. [Article]
- Novotny MJ, Frederickson WL, Waygood EB, Saier MH Jr: Allosteric regulation of glycerol kinase by enzyme IIIglc of the phosphotransferase system in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1985 May;162(2):810-6. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. doi: 10.1074/mcp.M111.012658. Epub 2011 Sep 9. [Article]
- Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ: Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science. 1993 Jan 29;259(5095):673-7. [Article]
- Feese M, Pettigrew DW, Meadow ND, Roseman S, Remington SJ: Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3544-8. [Article]
- Ormo M, Bystrom CE, Remington SJ: Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Biochemistry. 1998 Nov 24;37(47):16565-72. [Article]
- Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ: Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure. 1998 Nov 15;6(11):1407-18. [Article]
- Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ: Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion. Biochemistry. 1999 Mar 23;38(12):3508-18. [Article]
- Anderson MJ, DeLabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR: Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 --> Asp obtained using microfluidic crystallization devices. Biochemistry. 2007 May 15;46(19):5722-31. Epub 2007 Apr 19. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate experimental unknown target Details beta-D-fructofuranose 1,6-bisphosphate experimental unknown target Details