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Cite: NAR/gkaa742 2020



PUL General Information

Literature Information

PUL ID

PUL0596

PubMed

25388295, Mol Microbiol. 2015 Jan;95(2):209-30. doi: 10.1111/mmi.12859. Epub 2014 Dec 19.

Characterization method

enzyme activity assay,qPCR,crystallization

Genomic accession number

FP929042

Nucelotide position range

196460-202017

Substrate

starch

Loci

EUR_01830-01860

Species

[Eubacterium] rectale/39491

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

- EUR_01830 CBK89421.1 0 - 1269 (+) FP929042.1:196460-197729 -
- EUR_01840 CBK89422.1 1371 - 2751 (+) FP929042.1:197831-199211 -
- EUR_01850 CBK89423.1 2750 - 3638 (+) FP929042.1:199210-200098 -
- EUR_01860 CBK89424.1 3863 - 5558 (+) FP929042.1:200323-202018 3.2.1.1

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 1269 (+) STP: STP|SBP_bac_1 No
- 1372 - 2751 (+) TC: gnl|TC-DB|Q8DT27|3.A.1.1.27 Yes
- 2751 - 3638 (+) TC: gnl|TC-DB|Q8DT26|3.A.1.1.27 Yes
- 3864 - 5558 (+) CAZyme: GH13_36 Yes

PUL ID

PUL0596

PubMed

25388295, Mol Microbiol. 2015 Jan;95(2):209-30. doi: 10.1111/mmi.12859. Epub 2014 Dec 19.

Title

Molecular details of a starch utilization pathway in the human gut symbiont Eubacterium rectale.

Author

Cockburn DW, Orlovsky NI, Foley MH, Kwiatkowski KJ, Bahr CM, Maynard M, Demeler B, Koropatkin NM

Abstract

Eubacterium rectale is a prominent human gut symbiont yet little is known about the molecular strategies this bacterium has developed to acquire nutrients within the competitive gut ecosystem. Starch is one of the most abundant glycans in the human diet, and E. rectale increases in vivo when the host consumes a diet rich in resistant starch, although it is not a primary degrader of this glycan. Here we present the results of a quantitative proteomics study in which we identify two glycoside hydrolase 13 family enzymes, and three ABC transporter solute-binding proteins that are abundant during growth on starch and, we hypothesize, work together at the cell surface to degrade starch and capture the released maltooligosaccharides. EUR_21100 is a multidomain cell wall anchored amylase that preferentially targets starch polysaccharides, liberating maltotetraose, whereas the membrane-associated maltogenic amylase EUR_01860 breaks down maltooligosaccharides longer than maltotriose. The three solute-binding proteins display a range of glycan-binding specificities that ensure the capture of glucose through maltoheptaose and some alpha1,6-branched glycans. Taken together, we describe a pathway for starch utilization by E. rectale DSM 17629 that may be conserved among other starch-degrading Clostridium cluster XIVa organisms in the human gut.