PUL ID

PUL0588

PubMed

23278377, FEMS Microbiol Lett. 2013 Mar;340(1):33-40. doi: 10.1111/1574-6968.12069. Epub 2013 Jan 16.

Characterization method

enzyme activity assay,RT-PCR

Genomic accession number

AL645882.2

Nucelotide position range

5692292-5696970

Substrate

chitin

Loci

SCO5232-SCO5235

Species

Streptomyces coelicolor/1902

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

SCO5232 - CAB94617.1 0 - 1278 (+) AL645882.2:5692292-5693570 -
SCO5233 - CAB94618.1 1366 - 2353 (+) AL645882.2:5693658-5694645 -
SCO5234 - CAB94619.1 2349 - 3180 (+) AL645882.2:5694641-5695472 -
SCO5235 - CAB94620.1 3188 - 4679 (+) AL645882.2:5695480-5696971 -

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 1278 (+) TC: gnl|TC-DB|Q8KN19|3.A.1.1.33 Yes
- 1367 - 2353 (+) TC: gnl|TC-DB|Q8KN18|3.A.1.1.33 Yes
- 2350 - 3180 (+) TC: gnl|TC-DB|Q8KN17|3.A.1.1.33 Yes
- 3189 - 4679 (+) CAZyme: GH3 Yes

PUL ID

PUL0588

PubMed

23278377, FEMS Microbiol Lett. 2013 Mar;340(1):33-40. doi: 10.1111/1574-6968.12069. Epub 2013 Jan 16.

Title

Enzymatic and genetic characterization of the DasD protein possessing N-acetyl-beta-d-glucosaminidase activity in Streptomyces coelicolor A3(2).

Author

Saito A, Ebise H, Orihara Y, Murakami S, Sano Y, Kimura A, Sugiyama Y, Ando A, Fujii T, Miyashita K

Abstract

The dasD gene is located just downstream of the dasABC gene cluster, encoding components of an ABC transporter for uptake of a chitin-degradation product N,N'-diacetylchitobiose [(GlcNAc)(2) ] in Streptomyces coelicolor A3(2). To clarify the roles of the DasD protein in the degradation and assimilation of chitin, we obtained and characterized a recombinant DasD protein and a dasD-null mutant of S. coelicolor A3(2). The recombinant DasD protein produced in Escherichia coli showed N-acetyl-beta-d-glucosaminidase (GlcNAcase) activity and its optimum temperature and pH were 40 degrees C and 7, respectively. dasD transcription was strongly induced in the presence of chitin, weakly by chitosan, but not by cellulose or xylan in S. coelicolor A3(2). Immuno-blot analysis demonstrated that DasD is a cytoplasmic protein. The dasD-null mutant exhibited cellular GlcNAcase activity which was comparable with that of the parent strain M145. DasD, thus, did not seem to be a major GlcNAcase. Induced extracellular chitinase activity in the dasD-null mutant was, interestingly, higher than M145, in the presence of colloidal chitin or (GlcNAc)(2) . In contrast to M145, (GlcNAc)(2) temporally accumulated in the culture supernatant of the dasD-null mutant in the presence of colloidal chitin.