Lysine decarboxylase, inducible (P0A9H3)

Identification
Name:Lysine decarboxylase, inducible
Synonyms:
  • LDC
Gene Name:cadA
Enzyme Class:
Biological Properties
General Function:Involved in carboxy-lyase activity
Specific Function:Appears to play a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0L-Lysine ↔ 1.0Cadaverine + 1.0Carbon dioxide
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Lysine ↔ 1.0Cadaverine + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0L-Lysine+1.0Thumb → 1.0Thumb
1.0L-Lysine + 1.0L-Lysine → 1.0Cadaverine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0L-Lysine ↔ 1.0Cadaverine + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB02322CadaverineMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00182L-LysineMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
cofactor binding
lyase activity
pyridoxal phosphate binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b4131
Gene OrientationCounterclockwise
Centisome Percentage:93.85
Left Sequence End4354493
Right Sequence End4356640
Gene Sequence:
>2148 bp
ATGAACGTTATTGCAATATTGAATCACATGGGGGTTTATTTTAAAGAAGAACCCATCCGT
GAACTTCATCGCGCGCTTGAACGTCTGAACTTCCAGATTGTTTACCCGAACGACCGTGAC
GACTTATTAAAACTGATCGAAAACAATGCGCGTCTGTGCGGCGTTATTTTTGACTGGGAT
AAATATAATCTCGAGCTGTGCGAAGAAATTAGCAAAATGAACGAGAACCTGCCGTTGTAC
GCGTTCGCTAATACGTATTCCACTCTCGATGTAAGCCTGAATGACCTGCGTTTACAGATT
AGCTTCTTTGAATATGCGCTGGGTGCTGCTGAAGATATTGCTAATAAGATCAAGCAGACC
ACTGACGAATATATCAACACTATTCTGCCTCCGCTGACTAAAGCACTGTTTAAATATGTT
CGTGAAGGTAAATATACTTTCTGTACTCCTGGTCACATGGGCGGTACTGCATTCCAGAAA
AGCCCGGTAGGTAGCCTGTTCTATGATTTCTTTGGTCCGAATACCATGAAATCTGATATT
TCCATTTCAGTATCTGAACTGGGTTCTCTGCTGGATCACAGTGGTCCACACAAAGAAGCA
GAACAGTATATCGCTCGCGTCTTTAACGCAGACCGCAGCTACATGGTGACCAACGGTACT
TCCACTGCGAACAAAATTGTTGGTATGTACTCTGCTCCAGCAGGCAGCACCATTCTGATT
GACCGTAACTGCCACAAATCGCTGACCCACCTGATGATGATGAGCGATGTTACGCCAATC
TATTTCCGCCCGACCCGTAACGCTTACGGTATTCTTGGTGGTATCCCACAGAGTGAATTC
CAGCACGCTACCATTGCTAAGCGCGTGAAAGAAACACCAAACGCAACCTGGCCGGTACAT
GCTGTAATTACCAACTCTACCTATGATGGTCTGCTGTACAACACCGACTTCATCAAGAAA
ACACTGGATGTGAAATCCATCCACTTTGACTCCGCGTGGGTGCCTTACACCAACTTCTCA
CCGATTTACGAAGGTAAATGCGGTATGAGCGGTGGCCGTGTAGAAGGGAAAGTGATTTAC
GAAACCCAGTCCACTCACAAACTGCTGGCGGCGTTCTCTCAGGCTTCCATGATCCACGTT
AAAGGTGACGTAAACGAAGAAACCTTTAACGAAGCCTACATGATGCACACCACCACTTCT
CCGCACTACGGTATCGTGGCGTCCACTGAAACCGCTGCGGCGATGATGAAAGGCAATGCA
GGTAAGCGTCTGATCAACGGTTCTATTGAACGTGCGATCAAATTCCGTAAAGAGATCAAA
CGTCTGAGAACGGAATCTGATGGCTGGTTCTTTGATGTATGGCAGCCGGATCATATCGAT
ACGACTGAATGCTGGCCGCTGCGTTCTGACAGCACCTGGCACGGCTTCAAAAACATCGAT
AACGAGCACATGTATCTTGACCCGATCAAAGTCACCCTGCTGACTCCGGGGATGGAAAAA
GACGGCACCATGAGCGACTTTGGTATTCCGGCCAGCATCGTGGCGAAATACCTCGACGAA
CATGGCATCGTTGTTGAGAAAACCGGTCCGTATAACCTGCTGTTCCTGTTCAGCATCGGT
ATCGATAAGACCAAAGCACTGAGCCTGCTGCGTGCTCTGACTGACTTTAAACGTGCGTTC
GACCTGAACCTGCGTGTGAAAAACATGCTGCCGTCTCTGTATCGTGAAGATCCTGAATTC
TATGAAAACATGCGTATTCAGGAACTGGCTCAGAATATCCACAAACTGATTGTTCACCAC
AATCTGCCGGATCTGATGTATCGCGCATTTGAAGTGCTGCCGACGATGGTAATGACTCCG
TATGCTGCATTCCAGAAAGAGCTGCACGGTATGACCGAAGAAGTTTACCTCGACGAAATG
GTAGGTCGTATTAACGCCAATATGATCCTTCCGTACCCGCCGGGAGTTCCTCTGGTAATG
CCGGGTGAAATGATCACCGAAGAAAGCCGTCCGGTTCTGGAGTTCCTGCAGATGCTGTGT
GAAATCGGCGCTCACTATCCGGGCTTTGAAACCGATATTCACGGTGCATACCGTCAGGCT
GATGGCCGCTATACCGTTAAGGTATTGAAAGAAGAAAGCAAAAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:715
Protein Molecular Weight:81260
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Lysine decarboxylase, inducible
MNVIAILNHMGVYFKEEPIRELHRALERLNFQIVYPNDRDDLLKLIENNARLCGVIFDWD
KYNLELCEEISKMNENLPLYAFANTYSTLDVSLNDLRLQISFFEYALGAAEDIANKIKQT
TDEYINTILPPLTKALFKYVREGKYTFCTPGHMGGTAFQKSPVGSLFYDFFGPNTMKSDI
SISVSELGSLLDHSGPHKEAEQYIARVFNADRSYMVTNGTSTANKIVGMYSAPAGSTILI
DRNCHKSLTHLMMMSDVTPIYFRPTRNAYGILGGIPQSEFQHATIAKRVKETPNATWPVH
AVITNSTYDGLLYNTDFIKKTLDVKSIHFDSAWVPYTNFSPIYEGKCGMSGGRVEGKVIY
ETQSTHKLLAAFSQASMIHVKGDVNEETFNEAYMMHTTTSPHYGIVASTETAAAMMKGNA
GKRLINGSIERAIKFRKEIKRLRTESDGWFFDVWQPDHIDTTECWPLRSDSTWHGFKNID
NEHMYLDPIKVTLLTPGMEKDGTMSDFGIPASIVAKYLDEHGIVVEKTGPYNLLFLFSIG
IDKTKALSLLRALTDFKRAFDLNLRVKNMLPSLYREDPEFYENMRIQELAQNIHKLIVHH
NLPDLMYRAFEVLPTMVMTPYAAFQKELHGMTEEVYLDEMVGRINANMILPYPPGVPLVM
PGEMITEESRPVLEFLQMLCEIGAHYPGFETDIHGAYRQADGRYTVKVLKEESKK
References
External Links:
ResourceLink
Uniprot ID:P0A9H3
Uniprot Name:LDCI_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676884
Ecogene ID:EG10131
Ecocyc:EG10131
ColiBase:b4131
Kegg Gene:b4131
EchoBASE ID:EB0129
CCDB:LDCI_ECOLI
BacMap:16131957
General Reference:
  • Auger, E. A., Redding, K. E., Plumb, T., Childs, L. C., Meng, S. Y., Bennett, G. N. (1989). "Construction of lac fusions to the inducible arginine- and lysine decarboxylase genes of Escherichia coli K12." Mol Microbiol 3:609-620. Pubmed: 2527331
  • 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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • 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
  • Meng, S. Y., Bennett, G. N. (1992). "Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH." J Bacteriol 174:2659-2669. Pubmed: 1556085
  • Sabo, D. L., Fischer, E. H. (1974). "Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5'-phosphate binding site." Biochemistry 13:670-676. Pubmed: 4204273
  • Snider, J., Gutsche, I., Lin, M., Baby, S., Cox, B., Butland, G., Greenblatt, J., Emili, A., Houry, W. A. (2006). "Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase." J Biol Chem 281:1532-1546. Pubmed: 16301313
  • Watson, N., Dunyak, D. S., Rosey, E. L., Slonczewski, J. L., Olson, E. R. (1992). "Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH." J Bacteriol 174:530-540. Pubmed: 1370290