4-hydroxy-tetrahydrodipicolinate reductase

Details

Name
4-hydroxy-tetrahydrodipicolinate reductase
Synonyms
  • 1.17.1.8
  • HTPA reductase
Gene Name
dapB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011432|4-hydroxy-tetrahydrodipicolinate reductase
MHDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGV
TVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAAD
IAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAH
ALDKDLKDCAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSR
MTFANGAVRSALWLSGKESGLFDMRDVLDLNNL
Number of residues
273
Molecular Weight
28756.34
Theoretical pI
5.55
GO Classification
Functions
4-hydroxy-tetrahydrodipicolinate reductase / identical protein binding / NAD binding / NADP binding / oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
Processes
cellular amino acid biosynthetic process / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate
Components
cytosol
General Function
Oxidoreductase activity, acting on ch or ch2 groups, nad or nadp as acceptor
Specific Function
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011433|4-hydroxy-tetrahydrodipicolinate reductase (dapB)
ATGCATGATGCAAACATCCGCGTTGCCATCGCGGGAGCCGGGGGGCGTATGGGCCGCCAG
TTGATTCAGGCGGCGCTGGCATTAGAGGGCGTGCAGTTGGGCGCTGCGCTGGAGCGTGAA
GGATCTTCTTTACTGGGCAGCGACGCCGGTGAGCTGGCCGGAGCCGGGAAAACAGGCGTT
ACCGTGCAAAGCAGCCTCGATGCGGTAAAAGATGATTTTGATGTGTTTATCGATTTTACC
CGTCCGGAAGGTACGCTGAACCATCTCGCTTTTTGTCGCCAGCATGGCAAAGGGATGGTG
ATCGGCACTACGGGGTTTGACGAAGCCGGTAAACAAGCAATTCGTGACGCCGCTGCCGAT
ATTGCGATTGTCTTTGCTGCCAATTTTAGCGTTGGCGTTAACGTCATGCTTAAGCTGCTG
GAGAAAGCAGCCAAAGTGATGGGTGACTACACCGATATCGAAATTATTGAAGCACATCAT
AGACATAAAGTTGATGCGCCGTCAGGCACCGCACTGGCAATGGGAGAGGCGATCGCCCAC
GCCCTTGATAAAGATCTGAAAGATTGCGCGGTCTACAGTCGTGAAGGCCACACCGGTGAA
CGTGTGCCTGGCACCATTGGTTTTGCCACCGTGCGTGCAGGTGACATCGTTGGTGAACAT
ACCGCGATGTTTGCCGATATTGGCGAGCGTCTGGAGATCACCCATAAGGCGTCCAGCCGT
ATGACATTTGCTAACGGCGCGGTAAGATCGGCTTTGTGGTTGAGTGGTAAGGAAAGCGGT
CTTTTTGATATGCGAGATGTACTTGATCTCAATAATTTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04036
UniProtKB Entry NameDAPB_ECOLI
GenBank Protein ID145710
GenBank Gene IDM10611
General References
  1. Bouvier J, Richaud C, Richaud F, Patte JC, Stragier P: Nucleotide sequence and expression of the Escherichia coli dapB gene. J Biol Chem. 1984 Dec 10;259(23):14829-34. [Article]
  2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [Article]
  3. 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]
  4. 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]
  5. Bouvier J, Patte JC, Stragier P: Multiple regulatory signals in the control region of the Escherichia coli carAB operon. Proc Natl Acad Sci U S A. 1984 Jul;81(13):4139-43. [Article]
  6. Reddy SG, Sacchettini JC, Blanchard JS: Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase. Biochemistry. 1995 Mar 21;34(11):3492-501. [Article]
  7. Bouvier J, Stragier P, Morales V, Remy E, Gutierrez C: Lysine represses transcription of the Escherichia coli dapB gene by preventing its activation by the ArgP activator. J Bacteriol. 2008 Aug;190(15):5224-9. doi: 10.1128/JB.01782-07. Epub 2008 May 23. [Article]
  8. Devenish SR, Blunt JW, Gerrard JA: NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J Med Chem. 2010 Jun 24;53(12):4808-12. doi: 10.1021/jm100349s. [Article]
  9. Scapin G, Blanchard JS, Sacchettini JC: Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry. 1995 Mar 21;34(11):3502-12. [Article]
  10. Reddy SG, Scapin G, Blanchard JS: Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Biochemistry. 1996 Oct 15;35(41):13294-302. [Article]
  11. Scapin G, Reddy SG, Zheng R, Blanchard JS: Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry. 1997 Dec 9;36(49):15081-8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB033633-Acetylpyridine Adenine DinucleotideexperimentalunknownDetails
DB04267Dipicolinic acidexperimentalunknownDetails