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Cite: NAR/gkaa742 2020

Because CGCFinder predicted no CGC for this PUL, the gene cluster depicted below contains dbCAN2 and CGC signature predictions for all genes in the PUL, instead of a predicted CGC.


PUL General Information

Literature Information

PUL ID

PUL0497

PubMed

11772635, Appl Environ Microbiol. 2002 Jan;68(1):263-70. doi: 10.1128/AEM.68.1.263-270.2002.

Characterization method

clone and expression,enzyme activity assay

Genomic accession number

AB063629.1

Nucelotide position range

537-7768

Substrate

chitin

Loci

chiD-cbp1-chiA

Species

Pseudoalteromonas piscicida/43662

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

chiD - BAB79618.1 0 - 3150 (+) AB063629.1:537-3687 -
cbp1 - BAB79619.1 3159 - 4609 (+) AB063629.1:3696-5146 -
chiA - BAB79620.1 4639 - 7232 (+) AB063629.1:5176-7769 -

Cluster number

0

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 3114 (+) CAZyme: CBM5|GH18 No
- 3160 - 4587 (+) CAZyme: CBM5|AA10 No
- 4640 - 7102 (+) CAZyme: CBM5|GH18 No

PUL ID

PUL0497

PubMed

11772635, Appl Environ Microbiol. 2002 Jan;68(1):263-70. doi: 10.1128/AEM.68.1.263-270.2002.

Title

Identification and characterization of the gene cluster involved in chitin degradation in a marine bacterium, Alteromonas sp. strain O-7.

Author

Tsujibo H, Orikoshi H, Baba N, Miyahara M, Miyamoto K, Yasuda M, Inamori Y

Abstract

Alteromonas sp. strain O-7 secretes chitinase A (ChiA), chitinase B (ChiB), and chitinase C (ChiC) in the presence of chitin. A gene cluster involved in the chitinolytic system of the strain was cloned and sequenced upstream of and including the chiA gene. The gene cluster consisted of three different open reading frames organized in the order chiD, cbp1, and chiA. The chiD, cbp1, and chiA genes were closely linked and transcribed in the same direction. Sequence analysis indicated that Cbp1 (475 amino acids) was a chitin-binding protein composed of two discrete functional regions. ChiD (1,037 amino acids) showed sequence similarity to bacterial chitinases classified into family 18 of glycosyl hydrolases. The cbp1 and chiD genes were expressed in Escherichia coli, and the recombinant proteins were purified to homogeneity. The highest binding activities of Cbp1 and ChiD were observed when alpha-chitin was used as a substrate. Cbp1 and ChiD possessed a chitin-binding domain (ChtBD) belonging to ChtBD type 3. ChiD rapidly hydrolyzed chitin oligosaccharides in sizes from trimers to hexamers, but not chitin. However, after prolonged incubation with large amounts of ChiD, the enzyme produced a small amount of (GlcNAc)(2) from chitin. The optimum temperature and pH of ChiD were 50 degrees C and 7.0, respectively.