Periplasmic trehalase (P13482)

Identification
Name:Periplasmic trehalase
Synonyms:
  • Alpha,alpha-trehalase
  • Alpha,alpha-trehalose glucohydrolase
Gene Name:treA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system
Cellular Location:Periplasm
SMPDB Pathways:
  • Secondary metabolites: Trehalose Biosynthesis and Metabolism PW000968
  • Starch and sucrose metabolism PW000941
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 2.0Thumb
1.0Trehalose + 1.0Water ↔ 2.0D-Glucose
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Trehalose + 1.0Water ↔ 1.0b-D-Glucose + 1.0alpha-D-Glucose
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Trehalose + 1.0Water → 1.0b-D-Glucose + 1.0D-Glucose
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 2.0Thumb
1.0Water + 1.0Trehalose → 2.0D-Glucose
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Trehalose + 1.0Water → 1.0b-D-Glucose + 1.0alpha-D-Glucose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB03345alpha-D-GlucoseMetaboCard
ECMDB00516b-D-GlucoseMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB00975TrehaloseMetaboCard
ECMDB00494WaterMetaboCard
ECMDB24256α,α-trehaloseMetaboCard
GO Classification:
Function
alpha,alpha-trehalase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
trehalase activity
Process
carbohydrate metabolic process
disaccharide metabolic process
metabolic process
oligosaccharide metabolic process
primary metabolic process
trehalose metabolic process
Gene Properties
Blattner:b1197
Gene OrientationCounterclockwise
Centisome Percentage:26.83
Left Sequence End1244902
Right Sequence End1246599
Gene Sequence:
>1698 bp
ATGAAATCCCCCGCACCTTCTCGCCCGCAAAAAATGGCGTTAATTCCAGCCTGTATCTTT
TTGTGTTTCGCTGCGCTATCGGTGCAGGCAGAAGAAACACCGGTAACACCACAGCCGCCT
GATATTTTATTAGGGCCGCTGTTTAATGATGTGCAAAACGCCAAACTTTTTCCGGACCAA
AAAACCTTTGCCGATGCCGTGCCGAACAGCGATCCGCTGATGATCCTTGCTGATTATCGG
ATGCAGCAAAACCAGAGCGGATTTGATCTGCGCCATTTCGTTAACGTCAATTTCACCCTG
CCGAAAGAAGGCGAGAAATATGTTCCGCCAGAGGGGCAGTCACTGCGCGAACATATTGAC
GGACTTTGGCCGGTATTAACGCGTTCTACCGAAAACACCGAAAAATGGGATTCTCTGTTA
CCGCTGCCGGAACCTTATGTCGTGCCGGGCGGACGCTTTCGCGAGGTATATTACTGGGAC
AGTTACTTCACCATGTTAGGACTTGCCGAAAGCGGTCACTGGGATAAAGTCGCGGATATG
GTGGCCAATTTTGCTCATGAAATAGACACTTACGGTCATATTCCCAACGGCAACCGCAGT
TACTATTTAAGCCGCTCGCAACCGCCCTTCTTTGCCCTGATGGTAGAGTTACTGGCGCAG
CATGAAGGCGATGCCGCGTTGAAGCAATACCTGCCGCAAATGCAAAAAGAATATGCTTAC
TGGATGGACGGTGTTGAAAACCTGCAAGCCGGACAACAGGAAAAACGCGTTGTCAAACTT
CAGGATGGTACCCTTCTCAACCGCTACTGGGACGATCGCGATACGCCACGACCAGAGTCA
TGGGTGGAAGATATTGCCACCGCCAAAAGCAATCCGAATCGACCTGCCACTGAAATTTAC
CGCGACCTGCGCTCTGCCGCTGCGTCTGGCTGGGATTTCAGCTCGCGCTGGATGGACAAC
CCGCAGCAGTTAAATACCTTACGCACCACCAGCATCGTACCGGTCGATCTGAACAGCCTG
ATGTTTAAAATGGAAAAAATCCTCGCCCGCGCCAGCAAAGCTGCCGGAGATAACGCGATG
GCAAACCAGTACGAAACGCTGGCAAATGCCCGTCAAAAAGGGATCGAAAAATACCTGTGG
AACGATCAACAAGGCTGGTATGCCGATTACGACCTGAAAAGTCATAAAGTGCGCAATCAG
TTAACCGCGGCCGCCCTGTTCCCGCTGTACGTCAATGCGGCAGCGAAAGATCGCGCCAAC
AAAATGGCGACGGCGACGAAAACACATCTGCTGCAACCCGGCGGCCTGAACACCACGTCG
GTGAAAAGTGGGCAACAATGGGATGCGCCAAATGGCTGGGCACCGTTACAGTGGGTCGCG
ACAGAAGGATTACAAAACTACGGGCAAAAAGAGGTGGCGATGGACATTAGCTGGCACTTC
CTGACCAATGTTCAGCACACCTATGACCGGGAGAAAAAGCTGGTGGAAAAATATGATGTC
AGCACCACCGGAACGGGGGGCGGCGGTGGCGAATATCCATTACAGGATGGCTTTGGCTGG
ACCAATGGCGTGACGCTGAAAATGCTGGATTTGATCTGCCCGAAAGAGCAACCGTGTGAC
AATGTTCCGGCGACGCGTCCGACCGTTAAGTCAGCAACGACGCAACCCTCAACCAAAGAG
GCACAACCCACACCTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:565
Protein Molecular Weight:63636
Protein Theoretical pI:6
Signaling Regions:
  • 1-30
Transmembrane Regions:
  • None
Protein Sequence:
>Periplasmic trehalase
MKSPAPSRPQKMALIPACIFLCFAALSVQAEETPVTPQPPDILLGPLFNDVQNAKLFPDQ
KTFADAVPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHID
GLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADM
VANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAY
WMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIY
RDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSLMFKMEKILARASKAAGDNAM
ANQYETLANARQKGIEKYLWNDQQGWYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRAN
KMATATKTHLLQPGGLNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHF
LTNVQHTYDREKKLVEKYDVSTTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCD
NVPATRPTVKSATTQPSTKEAQPTP
References
External Links:
ResourceLink
Uniprot ID:P13482
Uniprot Name:TREA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651595
Ecogene ID:EG11017
Ecocyc:EG11017
ColiBase:b1197
Kegg Gene:b1197
EchoBASE ID:EB1010
CCDB:TREA_ECOLI
BacMap:16129160
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
  • Boos, W., Ehmann, U., Bremer, E., Middendorf, A., Postma, P. (1987). "Trehalase of Escherichia coli. Mapping and cloning of its structural gene and identification of the enzyme as a periplasmic protein induced under high osmolarity growth conditions." J Biol Chem 262:13212-13218. Pubmed: 2820965
  • Gutierrez, C., Ardourel, M., Bremer, E., Middendorf, A., Boos, W., Ehmann, U. (1989). "Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12." Mol Gen Genet 217:347-354. Pubmed: 2671658
  • 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
  • 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
  • Repoila, F., Gutierrez, C. (1991). "Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter." Mol Microbiol 5:747-755. Pubmed: 1710760