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 ID

PUL0567

PubMed

10220172, Microbiology (Reading). 1999 Apr;145 ( Pt 4):925-934. doi: 10.1099/13500872-145-4-925.

Characterization method

clone and expression,enzyme activity assay

Genomic accession number

AH007017.2

Nucelotide position range

89-8199

Substrate

chitin

Loci

chiABC

Species

Pseudoalteromonas sp. S9/55516

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

chiA - AAC79665.1 88 - 3253 (+) AH007017.2:177-3342 -
chiB - AAC79666.1 3496 - 5074 (+) AH007017.2:3585-5163 -
chiC - AAC79667.1 5589 - 8199 (+) AH007017.2:5678-8288 -

Cluster number

0

Gene name

Gene position

Gene type

Found by CGCFinder?

- 89 - 3253 (+) CAZyme: CBM5|GH18 No
- 3497 - 5074 (+) CAZyme: AA10|CBM5 No
- 5590 - 8199 (+) CAZyme: CBM5|GH18 No

PUL ID

PUL0567

PubMed

10220172, Microbiology (Reading). 1999 Apr;145 ( Pt 4):925-934. doi: 10.1099/13500872-145-4-925.

Title

Multiple genes involved in chitin degradation from the marine bacterium Pseudoalteromonas sp. strain S91.

Author

Techkarnjanaruk S, Goodman AE

Abstract

A cluster of three closely linked chitinase genes organized in the order chiA, chiB and chiC, with the same transcriptional direction, and two unlinked genes, chiP and chiQ, involved in chitin degradation in Pseudoalteromnas sp. strain S91 were cloned, sequenced and characterized. The deduced amino acid sequences revealed that ChiA, ChiB and ChiC exhibited similarities to chitinases belonging to family 18 of the glycosyl hydrolases while ChiP and ChiQ belonged to family 20. ChiP and ChiQ showed different enzymic activities against fluorescent chitin analogues, but neither was able to degrade colloidal chitin. ChiA possessed chitinase activity but did not bind chitin; ChiB bound chitin but had no chitinase activity; ChiC possessed strong chitinase activity and also bound chitin. Production of ChiC in S91 appeared to be controlled by chiA expression, since insertion of a transposon into the ORF of chiA resulted in the loss of chitinase activity as well as loss of ChiC proteins in a chitinase-negative mutant. In Escherichia coli, ChiC appeared to be expressed from its own promoter.