L-threonine 3-dehydrogenase (P07913)

Identification
Name:L-threonine 3-dehydrogenase
Synonyms:Not Available
Gene Name:tdh
Enzyme Class:
Biological Properties
General Function:Involved in zinc ion binding
Specific Function:L-threonine + NAD(+) = L-2-amino-3- oxobutanoate + NADH
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Glycine, serine and threonine metabolism ec00260
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0NAD + 1.0L-Threonine ↔ 1.0L-2-Amino-3-oxobutanoic acid + 1.0Hydrogen ion + 1.0NADH
ReactionCard
SMPDB Reactions:
1.0L-Threonine+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Threonine + 1.0NAD + 1.0L-Threonine → 1.0Hydrogen ion + 1.0NADH + 1.0L-2-Amino-3-oxobutanoic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0NAD + 1.0L-Threonine ↔ 1.0L-2-Amino-3-oxobutanoic acid + 1.0Hydrogen ion + 1.0NADH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Threonine + 1.0NAD → 1.0L-2-Amino-3-oxobutanoic acid + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB06454L-2-Amino-3-oxobutanoic acidMetaboCard
ECMDB00167L-ThreonineMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
ion binding
L-threonine 3-dehydrogenase activity
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
transition metal ion binding
zinc ion binding
Process
aspartate family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
oxidation reduction
threonine catabolic process
threonine metabolic process
Gene Properties
Blattner:b3616
Gene OrientationCounterclockwise
Centisome Percentage:81.65
Left Sequence End3788343
Right Sequence End3789368
Gene Sequence:
>1026 bp
ATGCCTTCAATTCGACTGGCTGATTTAGCGCAGCAGTTGGATGCAGAACTACACGGTGAT
GGCGATATCGTCATCACCGGCGTTGCGTCCATGCAATCTGCACAAACAGGTCACATTACG
TTCATGGTTAACCCAAAATACCGTGAGCATTTAGGCTTGTGCCAGGCGTCCGCGGTTGTC
ATGACCCAGGACGATCTTCCTTTCGCGAAAAGTGCCGCACTGGTAGTGAAGAATCCCTAC
CTGACTTACGCGCGCATGGCGCAAATTTTAGATACCACGCCGCAGCCCGCGCAGAACATT
GCACCCAGTGCGGTGATCGACGCGACGGCGAAGCTGGGTAACAACGTATCGATTGGCGCT
AACGCGGTGATTGAGTCCGGCGTTGAACTGGGCGATAACGTGATTATCGGTGCCGGTTGC
TTCGTAGGTAAAAACAGCAAAATCGGTGCAGGTTCGCGTCTCTGGGCGAACGTAACCATT
TACCATGAGATCCAGATCGGTCAGAATTGCCTGATCCAGTCCGGAACAGTGGTAGGCGCA
GACGGCTTTGGTTATGCCAACGATCGTGGTAACTGGGTGAAGATCCCACAGATTGGTCGC
GTAATTATTGGCGATCGCGTGGAGATCGGTGCCTGCACAACCATCGATCGCGGCGCGCTG
GATGACACTATTATTGGCAATGGCGTGATCATTGATAACCAGTGCCAGATTGCACATAAC
GTCGTGATTGGCGACAATACGGCGGTTGCCGGTGGCGTCATTATGGCGGGCAGCCTGAAA
ATTGGTCGTTACTGCATGATCGGCGGAGCCAGCGTAATCAACGGGCATATGGAAATATGC
GACAAAGTGACGGTTACGGGCATGGGTATGGTGATGCGTCCCATCACTGAACCAGGCGTC
TATTCCTCAGGCATTCCGCTGCAACCCAACAAAGTCTGGCGCAAAACCGCTGCACTGGTG
ATGAACATTGATGACATGAGCAAGCGTCTGAAATCGCTTGAGCGCAAGGTTAATCAACAA
GACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:341
Protein Molecular Weight:37239
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-threonine 3-dehydrogenase
MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMV
VGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGC
FAEYLVIPAFNAFKIPDNISDDLAAIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAA
AVAKHVGARNVVITDVNEYRLELARKMGITRAVNVAKENLNDVMAELGMTEGFDVGLEMS
GAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAA
LIQSGLDLSPIITHRFSIDDFQKGFDAMRSGQSGKVILSWD
References
External Links:
ResourceLink
Uniprot ID:P07913
Uniprot Name:TDH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902920
Ecogene ID:EG10993
Ecocyc:EG10993
ColiBase:b3616
Kegg Gene:b3616
EchoBASE ID:EB0986
CCDB:TDH_ECOLI
BacMap:16131487
General Reference:
  • Aronson, B. D., Somerville, R. L., Epperly, B. R., Dekker, E. E. (1989). "The primary structure of Escherichia coli L-threonine dehydrogenase." J Biol Chem 264:5226-5232. Pubmed: 2647748
  • 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
  • Epperly, B. R., Dekker, E. E. (1991). "L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies." J Biol Chem 266:6086-6092. Pubmed: 2007567
  • 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
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620