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
- Functionsdiaminopimelate decarboxylase activity / pyridoxal phosphate bindingProcesseslysine 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
Resource Link UniProtKB ID P00861 UniProtKB Entry Name DCDA_ECOLI GenBank Protein ID 455170 GenBank Gene ID J01614 - General References
- 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]
- 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]
- WHITE PJ, KELLY B: PURIFICATION AND PROPERTIES OF DIAMINOPIMELATE DECARBOXYLASE FROM ESCHERICHIA COLI. Biochem J. 1965 Jul;96:75-84. [Article]
- 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]
- 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]
- 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]
- 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]
- 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]