Aminoacyl-histidine dipeptidase (P15288)

Identification
Name:Aminoacyl-histidine dipeptidase
Synonyms:
  • Beta-alanyl-histidine dipeptidase
  • Carnosinase
  • Cysteinylglycinase
  • Peptidase D
  • Xaa-His dipeptidase
  • X-His dipeptidase
Gene Name:pepD
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity
Specific Function:Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cysteinylglycine + 1.0Water → 1.0L-Cysteine + 1.0Glycine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Cysteinylglycine + 1.0Water ↔ 1.0L-Cysteine + 1.0Glycine
ReactionCard
1.0R-S-Cysteinylglycine+1.0Thumb ↔ 1.0S-Substituted L-cysteine+1.0Thumb
1.0R-S-Cysteinylglycine + 1.0Water ↔ 1.0S-Substituted L-cysteine + 1.0Glycine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cysteinylglycine + 1.0Water → 1.0L-Cysteine + 1.0Glycine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0L-Prolinylglycine → 1.0Glycine + 1.0L-Proline
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Alanine-L-glutamate + 1.0Water → 1.0L-Alanine + 1.0L-Glutamate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00078CysteinylglycineMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB00161L-AlanineMetaboCard
ECMDB21242L-Alanine-L-glutamateMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00162L-ProlineMetaboCard
ECMDB21237L-ProlinylglycineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
hydrolase activity
protein binding
Process
macromolecule metabolic process
metabolic process
protein metabolic process
proteolysis
Gene Properties
Blattner:b0237
Gene OrientationCounterclockwise
Centisome Percentage:5.48
Left Sequence End254259
Right Sequence End255716
Gene Sequence:
>1458 bp
GTGTCTGAACTGTCTCAATTATCTCCACAGCCGCTGTGGGATATTTTTGCCAAAATCTGT
TCTATTCCTCACCCGTCCTATCATGAAGAGCAACTCGCTGAATACATTGTTGGTTGGGCA
AAAGAGAAAGGTTTCCATGTCGAACGCGATCAGGTAGGTAATATCCTGATTCGTAAACCT
GCTACCGCAGGTATGGAAAATCGTAAACCGGTCGTCTTACAGGCCCACCTCGATATGGTG
CCGCAGAAAAATAACGACACCGTGCATGACTTCACGAAAGATCCTATCCAGCCTTATATT
GATGGCGAATGGGTTAAAGCGCGCGGCACCACGCTGGGTGCGGATAACGGCATTGGTATG
GCCTCTGCGCTGGCGGTTCTGGCTGACGAAAACGTGGTTCACGGCCCGCTGGAAGTGCTG
CTGACCATGACCGAAGAAGCCGGTATGGACGGTGCGTTCGGCTTACAGGGCAACTGGTTG
CAGGCTGATATTCTGATTAACACCGACTCCGAAGAAGAAGGTGAAATCTACATGGGTTGT
GCGGGGGGTATCGACTTCACCTCCAACCTGCATTTAGATCGTGAAGCGGTTCCAGCTGGT
TTTGAAACCTTCAAGTTAACCTTAAAAGGTCTGAAAGGCGGTCACTCCGGCGGGGAAATC
CACGTTGGGCTGGGTAATGCCAACAAACTGCTGGTGCGCTTCCTGGCGGGTCATGCGGAA
GAACTGGATCTGCGCCTTATCGATTTCAACGGCGGCACACTGCGTAACGCCATCCCGCGT
GAAGCCTTTGCGACCATTGCTGTCGCAGCTGATAAAGTCGACGTCCTGAAATCTCTGGTG
AATACCTATCAGGAGATCCTGAAAAACGAGCTGGCAGAAAAAGAGAAAAATCTGGCCTTG
TTGCTGGACTCTGTAGCGAACGATAAAGCTGCCCTGATTGCGAAATCTCGCGATACCTTT
ATTCGTCTGCTGAACGCCACCCCGAACGGTGTGATTCGTAACTCCGATGTAGCCAAAGGT
GTGGTTGAAACCTCCCTGAACGTCGGTGTGGTGACCATGACTGACAATAACGTAGAAATT
CACTGCCTGATCCGTTCACTGATCGACAGCGGTAAAGACTACGTGGTGAGCATGCTGGAT
TCGCTGGGTAAACTGGCTGGCGCGAAAACCGAAGCGAAAGGCGCATATCCTGGCTGGCAG
CCGGACGCTAATTCTCCGGTGATGCATCTGGTACGTGAAACCTATCAGCGCCTGTTCAAC
AAGACGCCGAACATCCAGATTATCCACGCGGGCCTGGAATGTGGTCTGTTCAAAAAACCG
TATCCGGAAATGGACATGGTTTCTATCGGGCCAACTATCACCGGTCCACACTCTCCGGAT
GAGCAAGTTCACATCGAAAGCGTAGGTCATTACTGGACACTGCTGACTGAACTGCTGAAA
GAAATTCCGGCGAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:485
Protein Molecular Weight:52915
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aminoacyl-histidine dipeptidase
MSELSQLSPQPLWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVGNILIRKP
ATAGMENRKPVVLQAHLDMVPQKNNDTVHDFTKDPIQPYIDGEWVKARGTTLGADNGIGM
ASALAVLADENVVHGPLEVLLTMTEEAGMDGAFGLQGNWLQADILINTDSEEEGEIYMGC
AGGIDFTSNLHLDREAVPAGFETFKLTLKGLKGGHSGGEIHVGLGNANKLLVRFLAGHAE
ELDLRLIDFNGGTLRNAIPREAFATIAVAADKVDVLKSLVNTYQEILKNELAEKEKNLAL
LLDSVANDKAALIAKSRDTFIRLLNATPNGVIRNSDVAKGVVETSLNVGVVTMTDNNVEI
HCLIRSLIDSGKDYVVSMLDSLGKLAGAKTEAKGAYPGWQPDANSPVMHLVRETYQRLFN
KTPNIQIIHAGLECGLFKKPYPEMDMVSIGPTITGPHSPDEQVHIESVGHYWTLLTELLK
EIPAK
References
External Links:
ResourceLink
Uniprot ID:P15288
Uniprot Name:PEPD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902972
Ecogene ID:EG10695
Ecocyc:EG10695
ColiBase:b0237
Kegg Gene:b0237
EchoBASE ID:EB0689
CCDB:PEPD_ECOLI
BacMap:16128223
General Reference:
  • 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
  • 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
  • Henrich, B., Monnerjahn, U., Plapp, R. (1990). "Peptidase D gene (pepD) of Escherichia coli K-12: nucleotide sequence, transcript mapping, and comparison with other peptidase genes." J Bacteriol 172:4641-4651. Pubmed: 1695895
  • Henrich, B., Schroeder, U., Frank, R. W., Plapp, R. (1989). "Accurate mapping of the Escherichia coli pepD gene by sequence analysis of its 5' flanking region." Mol Gen Genet 215:369-373. Pubmed: 2651887
  • Schroeder, U., Henrich, B., Fink, J., Plapp, R. (1994). "Peptidase D of Escherichia coli K-12, a metallopeptidase of low substrate specificity." FEMS Microbiol Lett 123:153-159. Pubmed: 7988883
  • Suzuki, H., Kamatani, S., Kim, E. S., Kumagai, H. (2001). "Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12." J Bacteriol 183:1489-1490. Pubmed: 11157967
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842