3-methyl-2-oxobutanoate hydroxymethyltransferase (P31057)

Identification
Name:3-methyl-2-oxobutanoate hydroxymethyltransferase
Synonyms:
  • Ketopantoate hydroxymethyltransferase
  • KPHMT
Gene Name:panB
Enzyme Class:
Biological Properties
General Function:Involved in 3-methyl-2-oxobutanoate hydroxymethyltransferase activity
Specific Function:Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0alpha-Ketoisovaleric acid + 1.0Water + 1.05,10-Methylene-THF + 1.0a-Ketoisovaleric acid ↔ 1.02-Dehydropantoate + 1.0Tetrahydrofolic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0alpha-Ketoisovaleric acid + 1.0Water ↔ 1.0Tetrahydrofolic acid + 1.02-Dehydropantoate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.05,10-Methylene-THF+1.0Thumb+1.0Thumb → 1.0Tetrahydrofolic acid+1.02-dehydropantoate+1.0Thumb+1.0Thumb
1.0a-Ketoisovaleric acid + 1.05,10-Methylene-THF + 1.0Water + 1.05,10-Methylene-THF → 1.0Tetrahydrofolic acid + 1.02-dehydropantoate + 1.0Tetrahydrofolic acid + 1.02-Dehydropantoate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0alpha-Ketoisovaleric acid + 1.0Water + 1.05,10-Methylene-THF + 1.0a-Ketoisovaleric acid ↔ 1.02-Dehydropantoate + 1.0Tetrahydrofolic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0a-Ketoisovaleric acid + 1.0Water → 1.0Tetrahydrofolic acid + 1.02-Dehydropantoate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB040432-DehydropantoateMetaboCard
ECMDB013545,10-Methylene-THFMetaboCard
ECMDB00019a-Ketoisovaleric acidMetaboCard
ECMDB04092alpha-Ketoisovaleric acidMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
3-methyl-2-oxobutanoate hydroxymethyltransferase activity
catalytic activity
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
pantothenate biosynthetic process
Gene Properties
Blattner:b0134
Gene OrientationCounterclockwise
Centisome Percentage:3.21
Left Sequence End148807
Right Sequence End149601
Gene Sequence:
>795 bp
ATGAAACCGACCACCATCTCCTTACTGCAGAAGTACAAACAGGAAAAAAAACGTTTCGCG
ACCATCACCGCTTATGACTATAGCTTCGCCAAACTCTTTGCTGATGAAGGGCTTAACGTC
ATGCTGGTGGGCGATTCGCTGGGCATGACGGTTCAGGGGCACGACTCCACCCTGCCAGTT
ACCGTTGCCGATATCGCCTACCACACTGCCGCCGTACGTCGCGGCGCACCAAACTGCCTG
CTGCTGGCTGACCTGCCGTTTATGGCGTATGCCACGCCGGAACAAGCCTTCGAAAACGCC
GCAACGGTTATGCGTGCCGGTGCTAACATGGTCAAAATTGAAGGCGGTGAGTGGCTGGTA
GAAACCGTACAAATGCTGACCGAACGTGCCGTTCCTGTATGTGGTCACTTAGGTTTAACA
CCACAGTCAGTGAATATTTTCGGTGGCTACAAAGTTCAGGGGCGCGGCGATGAAGCGGGC
GATCAACTGCTCAGCGATGCATTAGCCTTAGAAGCTGCTGGGGCACAGCTGCTGGTGCTG
GAATGCGTGCCGGTTGAACTGGCAAAACGTATTACCGAAGCACTGGCGATCCCGGTTATT
GGCATTGGCGCAGGCAACGTCACTGACGGGCAGATCCTCGTGATGCACGACGCCTTTGGT
ATTACCGGCGGTCACATTCCTAAATTCGCTAAAAATTTCCTCGCCGAAACGGGCGACATC
CGCGCGGCTGTGCGGCAGTATATGGCTGAAGTGGAGTCCGGCGTTTATCCGGGCGAAGAA
CACAGTTTCCATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:264
Protein Molecular Weight:28237
Protein Theoretical pI:5
PDB File:1M3U
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-methyl-2-oxobutanoate hydroxymethyltransferase
MKPTTISLLQKYKQEKKRFATITAYDYSFAKLFADEGLNVMLVGDSLGMTVQGHDSTLPV
TVADIAYHTAAVRRGAPNCLLLADLPFMAYATPEQAFENAATVMRAGANMVKIEGGEWLV
ETVQMLTERAVPVCGHLGLTPQSVNIFGGYKVQGRGDEAGDQLLSDALALEAAGAQLLVL
ECVPVELAKRITEALAIPVIGIGAGNVTDGQILVMHDAFGITGGHIPKFAKNFLAETGDI
RAAVRQYMAEVESGVYPGEEHSFH
References
External Links:
ResourceLink
Uniprot ID:P31057
Uniprot Name:PANB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238990
PDB ID:1M3U
Ecogene ID:EG11675
Ecocyc:EG11675
ColiBase:b0134
Kegg Gene:b0134
EchoBASE ID:EB1626
CCDB:PANB_ECOLI
BacMap:16128127
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jones, C. E., Brook, J. M., Buck, D., Abell, C., Smith, A. G. (1993). "Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme." J Bacteriol 175:2125-2130. Pubmed: 8096212
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Powers, S. G., Snell, E. E. (1976). "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties." J Biol Chem 251:3786-3793. Pubmed: 6463
  • Teller, J. H., Powers, S. G., Snell, E. E. (1976). "Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis." J Biol Chem 251:3780-3785. Pubmed: 776976
  • von Delft, F., Inoue, T., Saldanha, S. A., Ottenhof, H. H., Schmitzberger, F., Birch, L. M., Dhanaraj, V., Witty, M., Smith, A. G., Blundell, T. L., Abell, C. (2003). "Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites." Structure 11:985-996. Pubmed: 12906829