Isoaspartyl peptidase (P37595)

Identification
Name:Isoaspartyl peptidase
Synonyms:
  • Beta-aspartyl-peptidase
  • EcAIII
  • Isoaspartyl dipeptidase
  • Isoaspartyl peptidase subunit alpha
  • Isoaspartyl peptidase subunit beta
Gene Name:iaaA
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity
Specific Function:May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:Not Available
SMPDB Reactions:
1.0L-Asparagine+1.0Thumb+1.0Thumb → 1.0L-Aspartic acid+1.0Thumb+1.0Thumb
1.0L-Asparagine + 1.0Water + 1.0L-Asparagine → 1.0L-Aspartic acid + 1.0Ammonium + 1.0L-Aspartic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Asparagine + 1.0Water → 1.0L-Aspartic acid + 1.0Ammonium
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21186AmmoniumMetaboCard
ECMDB00168L-AsparagineMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
Gene Properties
Blattner:b0828
Gene OrientationClockwise
Centisome Percentage:18.66
Left Sequence End865791
Right Sequence End866756
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:33394
Protein Theoretical pI:5
PDB File:1T3M
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Isoaspartyl peptidase
MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLL
EECPLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHV
MMIGEGAENFAFARGMERVSPEIFSTSLRYEQLLAARKEGATVLDHSGAPLDEKQKMGTV
GAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL
AAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWG
YAGDTPTTGIYREKGDTVATQ
References
External Links:
ResourceLink
Uniprot ID:P37595
Uniprot Name:IAAA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062400
PDB ID:1T3M
Ecogene ID:EG12407
Ecocyc:EG12407
ColiBase:b0828
Kegg Gene:b0828
EchoBASE ID:EB2307
CCDB:IAAA_ECOLI
BacMap:16128796
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
  • Borek, D., Jaskolski, M. (2000). "Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome." Acta Crystallogr D Biol Crystallogr 56:1505-1507. Pubmed: 11053866
  • Borek, D., Michalska, K., Brzezinski, K., Kisiel, A., Podkowinski, J., Bonthron, D. T., Krowarsch, D., Otlewski, J., Jaskolski, M. (2004). "Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog." Eur J Biochem 271:3215-3226. Pubmed: 15265041
  • Borodovsky, M., Rudd, K. E., Koonin, E. V. (1994). "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Nucleic Acids Res 22:4756-4767. Pubmed: 7984428
  • 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
  • Hejazi, M., Piotukh, K., Mattow, J., Deutzmann, R., Volkmer-Engert, R., Lockau, W. (2002). "Isoaspartyl dipeptidase activity of plant-type asparaginases." Biochem J 364:129-136. Pubmed: 11988085
  • Michalska, K., Borek, D., Hernandez-Santoyo, A., Jaskolski, M. (2008). "Crystal packing of plant-type L-asparaginase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 64:309-320. Pubmed: 18323626
  • Michalska, K., Brzezinski, K., Jaskolski, M. (2005). "Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate." J Biol Chem 280:28484-28491. Pubmed: 15946951
  • Nohno, T., Kasai, Y., Saito, T. (1988). "Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis." J Bacteriol 170:4097-4102. Pubmed: 3045084
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Parry, J., Clark, D. P. (2002). "Identification of a CysB-regulated gene involved in glutathione transport in Escherichia coli." FEMS Microbiol Lett 209:81-85. Pubmed: 12007658
  • Prahl, A., Pazgier, M., Hejazi, M., Lockau, W., Lubkowski, J. (2004). "Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli." Acta Crystallogr D Biol Crystallogr 60:1173-1176. Pubmed: 15159592