Aspartate 1-decarboxylase (P0A790)

Identification
Name:Aspartate 1-decarboxylase
Synonyms:
  • Aspartate alpha-decarboxylase
  • Aspartate 1-decarboxylase beta chain
  • Aspartate 1-decarboxylase alpha chain
Gene Name:panD
Enzyme Class:
Biological Properties
General Function:Involved in aspartate 1-decarboxylase activity
Specific Function:Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Hydrogen ion ↔ 1.0beta-Alanine + 1.0Carbon dioxide
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Aspartic acid ↔ 1.0beta-Alanine + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0L-Aspartic acid+1.0Thumb+1.0Thumb ? 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Hydrogen ion + 1.0L-Aspartic acid ? 1.0Carbon dioxide + 1.0beta-Alanine
ReactionCard
1.0L-Aspartic acid+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Hydrogen ion + 1.0L-Aspartic acid → 1.0Carbon dioxide + 1.0beta-Alanine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Hydrogen ion ↔ 1.0beta-Alanine + 1.0Carbon dioxide
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Aspartic acid → 1.0beta-Alanine + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00056beta-AlanineMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
GO Classification:
Function
aspartate 1-decarboxylase activity
binding
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
Process
alanine biosynthetic process
alanine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
pyruvate family amino acid metabolic process
Gene Properties
Blattner:b0131
Gene OrientationCounterclockwise
Centisome Percentage:3.15
Left Sequence End146314
Right Sequence End146694
Gene Sequence:
>381 bp
ATGATTCGCACGATGCTGCAGGGCAAACTCCACCGCGTGAAAGTGACTCATGCGGACCTG
CACTATGAAGGTTCTTGCGCCATTGACCAGGATTTTCTTGACGCAGCCGGTATTCTCGAA
AACGAAGCCATTGATATCTGGAATGTCACCAACGGCAAGCGTTTCTCCACTTATGCCATC
GCGGCAGAACGCGGTTCGAGAATTATTTCTGTTAACGGTGCGGCGGCCCACTGCGCCAGT
GTCGGCGATATTGTCATCATCGCCAGCTTCGTTACCATGCCAGATGAAGAAGCTCGCACC
TGGCGACCCAACGTCGCCTATTTTGAAGGCGACAATGAAATGAAACGTACCGCGAAAGCG
ATTCCGGTACAGGTTGCTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:126
Protein Molecular Weight:13834
Protein Theoretical pI:6
PDB File:1PQE
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartate 1-decarboxylase
MIRTMLQGKLHRVKVTHADLHYEGSCAIDQDFLDAAGILENEAIDIWNVTNGKRFSTYAI
AAERGSRIISVNGAAAHCASVGDIVIIASFVTMPDEEARTWRPNVAYFEGDNEMKRTAKA
IPVQVA
References
External Links:
ResourceLink
Uniprot ID:P0A790
Uniprot Name:PAND_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674346
PDB ID:1PQE
Ecogene ID:EG11747
Ecocyc:EG11747
ColiBase:b0131
Kegg Gene:b0131
EchoBASE ID:EB1697
CCDB:PAND_ECOLI
BacMap:16128124
General Reference:
  • Albert, A., Dhanaraj, V., Genschel, U., Khan, G., Ramjee, M. K., Pulido, R., Sibanda, B. L., von Delft, F., Witty, M., Blundell, T. L., Smith, A. G., Abell, C. (1998). "Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing." Nat Struct Biol 5:289-293. Pubmed: 9546220
  • 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
  • Cronan, J. E. Jr (1980). "Beta-alanine synthesis in Escherichia coli." J Bacteriol 141:1291-1297. Pubmed: 6767707
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • 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
  • Merkel, W. K., Nichols, B. P. (1996). "Characterization and sequence of the Escherichia coli panBCD gene cluster." FEMS Microbiol Lett 143:247-252. Pubmed: 8837478
  • Ramjee, M. K., Genschel, U., Abell, C., Smith, A. G. (1997). "Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry." Biochem J 323 ( Pt 3):661-669. Pubmed: 9169598
  • Saldanha, S. A., Birch, L. M., Webb, M. E., Nabbs, B. K., von Delft, F., Smith, A. G., Abell, C. (2001). "Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction." Chem Commun (Camb) :1760-1761. Pubmed: 12240302
  • Schmitzberger, F., Kilkenny, M. L., Lobley, C. M., Webb, M. E., Vinkovic, M., Matak-Vinkovic, D., Witty, M., Chirgadze, D. Y., Smith, A. G., Abell, C., Blundell, T. L. (2003). "Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase." EMBO J 22:6193-6204. Pubmed: 14633979