Xaa-Pro dipeptidase (P21165)

Identification
Name:Xaa-Pro dipeptidase
Synonyms:
  • X-Pro dipeptidase
  • Imidodipeptidase
  • Proline dipeptidase
  • Prolidase
Gene Name:pepQ
Enzyme Class:
Biological Properties
General Function:Involved in cellular process
Specific Function:Splits dipeptides with a prolyl residue in the C- terminal position and a polar or nonpolar amino acid at the N- terminal position. With much lower efficiency, also catalyzes the stereoselective hydrolysis of a wide variety of organophosphate triesters and organophosphonate diesters. Is able to hydrolyze the organophosphorus insecticide paraoxon and the p-nitrophenyl analogs of the nerve agents GB (sarin), GD (soman), GF, Vx and rVX
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Reactions:
1.0a dipeptide with proline at carboxy terminal+1.0Thumb ? 1.0Thumb+1.0a standard α amino acid
1.0a dipeptide with proline at carboxy terminal + 1.0Water ? 1.0L-Proline + 1.0a standard α amino acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00162L-ProlineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
metalloexopeptidase activity
metallopeptidase activity
peptidase activity
peptidase activity, acting on L-amino acid peptides
Process
cellular process
macromolecule metabolic process
metabolic process
protein metabolic process
proteolysis
Gene Properties
Blattner:b3847
Gene OrientationClockwise
Centisome Percentage:86.84
Left Sequence End4029184
Right Sequence End4030515
Gene Sequence:
>1332 bp
ATGCAACCGTCCAGAAACTTTGACGATCTCAAATTCTCCTCTATTCACCGCCGCATTTTG
CTGTGGGGAAGCGGTGGTCCGTTTCTGGATGGTTATGTACTGGTAATGATTGGCGTGGCG
CTGGAGCAACTGACGCCGGCGCTGAAACTGGACGCTGACTGGATTGGCTTGCTGGGCGCG
GGAACGCTCGCCGGGCTGTTCGTTGGCACATCGCTGTTTGGTTATATTTCCGATAAAGTC
GGACGGCGCAAAATGTTCCTCATTGATATCATCGCCATCGGCGTGATATCGGTGGCGACG
ATGTTTGTTTCATCCCCCGTCGAACTGTTGGTGATGCGGGTACTTATCGGCATTGTCATC
GGTGCAGATTATCCCATCGCCACCTCAATGATCACCGAGTTCTCCAGTACCCGTCAGCGG
GCGTTTTCCATCAGCTTTATTGCCGCGATGTGGTATGTCGGCGCGACCTGTGCCGATCTG
GTCGGCTACTGGCTTTATGATGTGGAAGGCGGCTGGCGCTGGATGCTGGGTAGCGCGGCG
ATCCCCTGTTTGTTGATTTTGATTGGTCGATTCGAACTGCCTGAATCTCCCCGCTGGTTA
TTACGCAAAGGGCGAGTAAAAGAGTGCGAAGAGATGATGATCAAACTGTTTGGCGAACCG
GTGGCTTTCGATGAAGAGCAGCCGCAGCAAACCCGTTTTCGCGATCTGTTTAATCGCCGC
CATTTTCCTTTTGTTCTGTTTGTTGCCGCCATCTGGACCTGCCAGGTGATCCCAATGTTC
GCCATTTACACCTTTGGCCCGCAAATCGTTGGTTTGTTGGGATTGGGGGTTGGCAAAAAC
GCGGCACTAGGGAATGTGGTGATTAGCCTGTTCTTTATGCTCGGCTGTATTCCGCCGATG
CTGTGGTTAAACACTGCCGGACGGCGTCCATTGTTGATTGGCAGCTTTGCCATGATGACG
CTGGCGCTGGCGGTTTTGGGGCTAATCCCGGATATGGGGATCTGGCTGGTAGTGATGGCC
TTTGCGGTGTATGCCTTTTTCTCTGGCGGGCCGGGTAATTTGCAGTGGCTCTATCCTAAT
GAACTCTTCCCGACAGATATCCGCGCCTCTGCCGTGGGCGTGATTATGTCCTTAAGTCGT
ATTGGCACCATTGTTTCGACCTGGGCACTACCGATCTTTATCAATAATTACGGTATCAGT
AACACGATGCTAATGGGGGCGGGTATCTCGCTGTTTGGCTTGTTGATTTCCGTAGCGTTT
GCCCCGGAGACTCGAGGGATGTCACTGGCGCAGACCAGCAATATGACGATCCGCGGGCAG
AGAATGGGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:443
Protein Molecular Weight:50176
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Xaa-Pro dipeptidase
MESLASLYKNHIATLQERTRDALARFKLDALLIHSGELFNVFLDDHPYPFKVNPQFKAWV
PVTQVPNCWLLVDGVNKPKLWFYLPVDYWHNVEPLPTSFWTEDVEVIALPKADGIGSLLP
AARGNIGYIGPVPERALQLGIEASNINPKGVIDYLHYYRSFKTEYELACMREAQKMAVNG
HRAAEEAFRSGMSEFDINIAYLTATGHRDTDVPYSNIVALNEHAAVLHYTKLDHQAPEEM
RSFLLDAGAEYNGYAADLTRTWSAKSDNDYAQLVKDVNDEQLALIATMKAGVSYVDYHIQ
FHQRIAKLLRKHQIITDMSEEAMVENDLTGPFMPHGIGHPLGLQVHDVAGFMQDDSGTHL
AAPAKYPYLRCTRILQPGMVLTIEPGIYFIESLLAPWREGQFSKHFNWQKIEALKPFGGI
RIEDNVVIHENNVENMTRDLKLA
References
External Links:
ResourceLink
Uniprot ID:P21165
Uniprot Name:PEPQ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674300
Ecogene ID:EG10698
Ecocyc:EG10698
ColiBase:b3847
Kegg Gene:b3847
EchoBASE ID:EB0692
CCDB:PEPQ_ECOLI
BacMap:16131693
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
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • 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
  • Nakahigashi, K., Inokuchi, H. (1990). "Nucleotide sequence between the fadB gene and the rrnA operon from Escherichia coli." Nucleic Acids Res 18:6439. Pubmed: 2243799
  • Park, M. S., Hill, C. M., Li, Y., Hardy, R. K., Khanna, H., Khang, Y. H., Raushel, F. M. (2004). "Catalytic properties of the PepQ prolidase from Escherichia coli." Arch Biochem Biophys 429:224-230. Pubmed: 15313226