Diaminopimelate decarboxylase

Details

Name
Diaminopimelate decarboxylase
Synonyms
  • 4.1.1.20
  • DAP decarboxylase
Gene Name
lysA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011324|Diaminopimelate decarboxylase
MPHSLFSTDTDLTAENLLRLPAEFGCPVWVYDAQIIRRQIAALKQFDVVRFAQKACSNIH
ILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTADVIDQATLERVSELQIPVN
AGSVDMLDQLGQVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYTDLPAALDVIQR
HHLQLVGIHMHIGSGVDYAHLEQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVD
TEHYYGLWNAAREQIARHLGHPVKLEIEPGRFLVAQSGVLITQVRSVKQMGSRHFVLVDA
GFNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQEGGNVETRA
LPEVKAGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDNGQARLIRRRQTIEELLALELL
Number of residues
420
Molecular Weight
46176.975
Theoretical pI
5.97
GO Classification
Functions
diaminopimelate decarboxylase activity / pyridoxal phosphate binding
Processes
lysine biosynthetic process via diaminopimelate
General Function
Pyridoxal phosphate binding
Specific Function
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011325|Diaminopimelate decarboxylase (lysA)
ATGCCACATTCACTGTTCAGCACCGATACCGATCTCACCGCCGAAAATCTGCTGCGTTTG
CCCGCTGAATTTGGCTGCCCGGTGTGGGTCTACGATGCGCAAATTATTCGTCGGCAGATT
GCAGCGCTGAAACAGTTTGATGTGGTGCGCTTTGCACAGAAAGCCTGTTCCAATATTCAT
ATTTTGCGCTTAATGCGTGAGCAGGGCGTGAAAGTGGATTCCGTCTCGTTAGGCGAAATA
GAGCGTGCGTTGGCGGCGGGTTACAATCCGCAAACGCACCCCGATGATATTGTTTTTACG
GCAGATGTTATCGATCAGGCGACGCTTGAACGCGTCAGTGAATTGCAAATTCCGGTGAAT
GCGGGTTCTGTTGATATGCTCGACCAACTGGGCCAGGTTTCGCCAGGGCATCGGGTATGG
CTGCGCGTTAATCCGGGGTTTGGTCACGGACATAGCCAAAAAACCAATACCGGTGGCGAA
AACAGCAAGCACGGTATCTGGTACACCGATCTGCCCGCCGCACTGGACGTGATACAACGT
CATCATCTGCAGCTGGTCGGCATTCACATGCACATTGGTTCTGGCGTTGATTATGCCCAT
CTGGAACAGGTGTGTGGTGCTATGGTGCGTCAGGTCATCGAATTCGGTCAGGATTTACAG
GCTATTTCTGCGGGCGGTGGGCTTTCTGTTCCTTATCAACAGGGTGAAGAGGCGGTTGAT
ACCGAACATTATTATGGTCTGTGGAATGCCGCGCGTGAGCAAATCGCCCGCCATTTGGGC
CACCCTGTGAAACTGGAAATTGAACCGGGTCGCTTCCTGGTAGCGCAGTCTGGCGTATTA
ATTACTCAGGTGCGGAGCGTCAAACAAATGGGGAGCCGCCACTTTGTGCTGGTTGATGCC
GGGTTCAACGATCTGATGCGCCCGGCAATGTACGGTAGTTACCACCATATCAGTGCCCTG
GCAGCTGATGGTCGTTCTCTGGAACACGCGCCAACGGTGGAAACCGTCGTCGCCGGACCG
TTATGTGAATCGGGCGATGTCTTTACCCAGCAGGAAGGGGGAAATGTTGAAACCCGCGCC
TTGCCGGAAGTGAAGGCAGGTGATTATCTGGTACTGCATGATACAGGGGCATATGGCGCA
TCAATGTCATCCAACTACAATAGCCGTCCGCTGTTACCAGAAGTTCTGTTTGATAATGGT
CAGGCGCGGTTGATTCGCCGTCGCCAGACCATCGAAGAATTACTGGCGCTGGAATTGCTT
TAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00861
UniProtKB Entry NameDCDA_ECOLI
GenBank Protein ID455170
GenBank Gene IDJ01614
General References
  1. Stragier P, Danos O, Patte JC: Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. II. Nucleotide sequence of the lysA gene and its regulatory region. J Mol Biol. 1983 Aug 5;168(2):321-31. [Article]
  2. 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]
  3. 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]
  4. WHITE PJ, KELLY B: PURIFICATION AND PROPERTIES OF DIAMINOPIMELATE DECARBOXYLASE FROM ESCHERICHIA COLI. Biochem J. 1965 Jul;96:75-84. [Article]
  5. Stragier P, Borne F, Richaud F, Richaud C, Patte JC: Regulatory pattern of the Escherichia coli lysA gene: expression of chromosomal lysA-lacZ fusions. J Bacteriol. 1983 Dec;156(3):1198-203. [Article]
  6. Stragier P, Richaud F, Borne F, Patte JC: Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. I. Identification of a lysR gene encoding an activator of the lysA gene. J Mol Biol. 1983 Aug 5;168(2):307-20. [Article]
  7. 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]
  8. Momany C, Levdikov V, Blagova L, Crews K: Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase. Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):549-52. Epub 2002 Feb 21. [Article]
  9. Hu T, Wu D, Chen J, Ding J, Jiang H, Shen X: The catalytic intermediate stabilized by a "down" active site loop for diaminopimelate decarboxylase from Helicobacter pylori. Enzymatic characterization with crystal structure analysis. J Biol Chem. 2008 Jul 25;283(30):21284-93. doi: 10.1074/jbc.M801823200. Epub 2008 May 28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03252D-LysineexperimentalunknownDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails