L-Ala-D/L-Glu epimerase (P51981)

Identification
Name:L-Ala-D/L-Glu epimerase
Synonyms:
  • AE epimerase
  • AEE
Gene Name:ycjG
Enzyme Class:Not Available
Biological Properties
General Function:Involved in cellular amino acid catabolic process
Specific Function:Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L- Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D- Ala-D-Ala
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Reactions:
1.0Thumb ? 1.0Thumb
1.0L-Ala-gamma-D-Glu ? 1.0L-Alanyl-L-Glutamate
ReactionCard
Complex Reactions:
1.0Thumb ↔ 1.0Thumb
1.0L-Alanyl-D-glutamate ↔ 1.0L-Alanine-L-glutamate
ReactionCard
1.0Thumb → 1.0Thumb
1.0L-Alanyl-D-glutamate → 1.0L-Alanyl-L-Glutamate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20574L-Ala-gamma-D-GluMetaboCard
ECMDB21242L-Alanine-L-glutamateMetaboCard
ECMDB21241L-Alanyl-D-glutamateMetaboCard
ECMDB20481L-Alanyl-L-GlutamateMetaboCard
GO Classification:
Function
catalytic activity
Process
cellular amino acid and derivative metabolic process
cellular amino acid catabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b1325
Gene OrientationClockwise
Centisome Percentage:29.89
Left Sequence End1386954
Right Sequence End1387919
Gene Sequence:
>966 bp
ATGGGCAAAGCAGTCATTGCAATTCATGGTGGCGCAGGTGCAATTAGCCGCGCGCAGATG
AGTCTGCAACAGGAATTACGCTACATCGAGGCGTTGTCTGCCATTGTTGAAACCGGGCAG
AAAATGCTGGAAGCGGGCGAAAGTGCGCTGGATGTGGTGACGGAAGCGGTGCGTCTGCTG
GAAGAGTGTCCACTGTTTAACGCCGGAATTGGCGCTGTCTTTACGCGTGATGAAACCCAT
GAACTGGACGCCTGTGTGATGGATGGTAACACCCTGAAAGCCGGTGCGGTGGCGGGCGTT
AGTCATCTGCGTAATCCGGTTCTTGCCGCCCGGCTGGTGATGGAGCAAAGCCCGCATGTG
ATGATGATTGGCGAAGGGGCAGAAAATTTTGCGTTTGCTCGTGGCATGGAGCGCGTCTCG
CCGGAGATTTTCTCCACGTCTTTGCGTTATGAACAACTACTGGCAGCGCGCAAGGAAGGG
GCAACCGTCCTCGACCATAGCGGTGCGCCACTGGATGAAAAACAGAAAATGGGCACCGTG
GGGGCCGTGGCGTTGGATTTAGACGGCAATTTGGCGGCAGCCACGTCCACAGGCGGAATG
ACCAATAAATTACCCGGACGAGTTGGCGATAGTCCCTTAGTGGGTGCCGGATGCTACGCC
AATAACGCCAGTGTGGCGGTTTCTTGTACCGGCACGGGCGAAGTCTTCATCCGCGCGCTG
GCGGCATATGACATCGCCGCGTTAATGGATTACGGCGGATTAAGTCTCGCGGAAGCCTGC
GAGCGGGTAGTAATGGAAAAACTCCCTGCGCTTGGCGGTAGCGGTGGCTTAATCGCTATC
GACCATGAAGGGAATGTCGCGCTACCGTTTAACACCGAAGGAATGTATCGCGCCTGGGGC
TACGCAGGCGATACGCCAACCACCGGTATCTACCGTGAAAAAGGGGACACCGTTGCCACA
CAGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:321
Protein Molecular Weight:34674
Protein Theoretical pI:5
PDB File:1JPD
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-Ala-D/L-Glu epimerase
MRTVKVFEEAWPLHTPFVIARGSRSEARVVVVELEEEGIKGTGECTPYPRYGESDASVMA
QIMSVVPQLEKGLTREELQKILPAGAARNALDCALWDLAARRQQQSLADLIGITLPETVI
TAQTVVIGTPDQMANSASTLWQAGAKLLKVKLDNHLISERMVAIRTAVPDATLIVDANES
WRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPLPICADESCHTRSNLKALKGR
YEMVNIKLDKTGGLTEALALATEARAQGFSLMLGCMLCTSRAISAALPLVPQVSFADLDG
PTWLAVDVEPALQFTTGELHL
References
External Links:
ResourceLink
Uniprot ID:P51981
Uniprot Name:AEEP_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062400
PDB ID:1JPD
Ecogene ID:EG13228
Ecocyc:EG13228
ColiBase:b1325
Kegg Gene:b1325
EchoBASE ID:EB3018
CCDB:AEEP_ECOLI
BacMap:90111249
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Cha, M. K., Kim, H. K., Kim, I. H. (1995). "Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli." J Biol Chem 270:28635-28641. Pubmed: 7499381
  • Gulick, A. M., Schmidt, D. M., Gerlt, J. A., Rayment, I. (2001). "Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis." Biochemistry 40:15716-15724. Pubmed: 11747448
  • 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
  • Park, J. T., Uehara, T. (2008). "How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)." Microbiol Mol Biol Rev 72:211-27, table of contents. Pubmed: 18535144
  • Schmidt, D. M., Hubbard, B. K., Gerlt, J. A. (2001). "Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases." Biochemistry 40:15707-15715. Pubmed: 11747447