3-methyl-2-oxobutanoate hydroxymethyltransferase
Details
- Name
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Synonyms
- 2.1.2.11
- Ketopantoate hydroxymethyltransferase
- KPHMT
- Gene Name
- panB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011244|3-methyl-2-oxobutanoate hydroxymethyltransferase MKPTTISLLQKYKQEKKRFATITAYDYSFAKLFADEGLNVMLVGDSLGMTVQGHDSTLPV TVADIAYHTAAVRRGAPNCLLLADLPFMAYATPEQAFENAATVMRAGANMVKIEGGEWLV ETVQMLTERAVPVCGHLGLTPQSVNIFGGYKVQGRGDEAGDQLLSDALALEAAGAQLLVL ECVPVELAKRITEALAIPVIGIGAGNVTDGQILVMHDAFGITGGHIPKFAKNFLAETGDI RAAVRQYMAEVESGVYPGEEHSFH
- Number of residues
- 264
- Molecular Weight
- 28237.235
- Theoretical pI
- 4.96
- GO Classification
- Functions3-methyl-2-oxobutanoate hydroxymethyltransferase activity / magnesium ion bindingProcessespantothenate biosynthetic process from valineComponentscytosol / membrane
- General Function
- Magnesium ion binding
- Specific Function
- Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.
- Pfam Domain Function
- Pantoate_transf (PF02548)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011245|3-methyl-2-oxobutanoate hydroxymethyltransferase (panB) ATGAAACCGACCACCATCTCCTTACTGCAGAAGTACAAACAGGAAAAAAAACGTTTCGCG ACCATCACCGCTTATGACTATAGCTTCGCCAAACTCTTTGCTGATGAAGGGCTTAACGTC ATGCTGGTGGGCGATTCGCTGGGCATGACGGTTCAGGGGCACGACTCCACCCTGCCAGTT ACCGTTGCCGATATCGCCTACCACACTGCCGCCGTACGTCGCGGCGCACCAAACTGCCTG CTGCTGGCTGACCTGCCGTTTATGGCGTATGCCACGCCGGAACAAGCCTTCGAAAACGCC GCAACGGTTATGCGTGCCGGTGCTAACATGGTCAAAATTGAAGGCGGTGAGTGGCTGGTA GAAACCGTACAAATGCTGACCGAACGTGCCGTTCCTGTATGTGGTCACTTAGGTTTAACA CCACAGTCAGTGAATATTTTCGGTGGCTACAAAGTTCAGGGGCGCGGCGATGAAGCGGGC GATCAACTGCTCAGCGATGCATTAGCCTTAGAAGCTGCTGGGGCACAGCTGCTGGTGCTG GAATGCGTGCCGGTTGAACTGGCAAAACGTATTACCGAAGCACTGGCGATCCCGGTTATT GGCATTGGCGCAGGCAACGTCACTGACGGGCAGATCCTCGTGATGCACGACGCCTTTGGT ATTACCGGCGGTCACATTCCTAAATTCGCTAAAAATTTCCTCGCCGAAACGGGCGACATC CGCGCGGCTGTGCGGCAGTATATGGCTGAAGTGGAGTCCGGCGTTTATCCGGGCGAAGAA CACAGTTTCCATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P31057 UniProtKB Entry Name PANB_ECOLI GenBank Protein ID 304927 GenBank Gene ID L17086 - General References
- Jones CE, Brook JM, Buck D, Abell C, Smith AG: Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme. J Bacteriol. 1993 Apr;175(7):2125-30. [Article]
- Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [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]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Teller JH, Powers SG, Snell EE: Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis. J Biol Chem. 1976 Jun 25;251(12):3780-5. [Article]
- Powers SG, Snell EE: Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties. J Biol Chem. 1976 Jun 25;251(12):3786-93. [Article]
- von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C: Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites. Structure. 2003 Aug;11(8):985-96. [Article]